We are analyzing https://link.springer.com/article/10.1186/1741-7007-10-62.

Title:
Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx | BMC Biology
Description:
Background The family of lysosome-associated membrane proteins (LAMP) comprises the multifunctional, ubiquitous LAMP-1 and LAMP-2, and the cell type-specific proteins DC-LAMP (LAMP-3), BAD-LAMP (UNC-46, C20orf103) and macrosialin (CD68). LAMPs have been implicated in a multitude of cellular processes, including phagocytosis, autophagy, lipid transport and aging. LAMP-2 isoform A acts as a receptor in chaperone-mediated autophagy. LAMP-2 deficiency causes the fatal Danon disease. The abundant proteins LAMP-1 and LAMP-2 are major constituents of the glycoconjugate coat present on the inside of the lysosomal membrane, the
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Science
Shopping
Education

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 8,170,236 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We're unsure if the website is profiting.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com might be making money, but it's not detectable how they're doing it.

Keywords {🔍}

lamp, pubmed, membrane, article, google, scholar, lysosomal, proteins, cas, figure, domain, structure, dclamp, domains, protein, cell, lysosomes, cells, central, biol, coat, transmembrane, human, glycoprotein, disulfide, glycosylated, molecular, luminal, residues, loop, conserved, models, molecules, structural, βsheet, saftig, authors, data, βprism, bond, regions, membranes, model, conformation, surface, mice, chain, full, autophagy, fold,

Topics {✒️}

joern krausze & konrad büssow x-ray diffraction data lamp-1/lamp-2 double-deficient fibroblasts article download pdf open access article cd208/dendritic cell-lysosomal β-strand pairs s2/s10 present pathogen-specific antigens multi-wavelength anomalous dispersion professional antigen-presenting cells c-type lectin fold c-terminal his6-tag left-handed α-helix c-terminal transmembrane helix de saint-vis n-acetyl-glucosamine residue x-linked vacuolar cardiomyopathy o-glycosylated 'hinge' region konrad büssow type i' β-turn membrane-proximal luminal domain lamp-2a transmembrane region pseudo β-prism structures n-linked glycosylation sites top view pseudo β-prism domains β-prism fold formed adjacent β-hairpin formed late endosome c-terminal cytosolic tail saccharide receptor-binding site cosen-binker li 'back' β-sheet consists bmc struct biol fluorescence-activated cell sorting dc-lamp domain consists similar n-glycosylated domains elongated β-strand conformation luminal region comprises o-glycan attachment sites carried sialylated o-glycans privacy choices/manage cookies authors’ original file initial β-strand conformation dc-lamp crystal structure article wilke n-acetylglucosamine residue connected high dc-lamp expression mccoy aj comprehensive python-based system

Questions {❓}

Jentoft N: Why are proteins O-glycosylated?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx
         description:The family of lysosome-associated membrane proteins (LAMP) comprises the multifunctional, ubiquitous LAMP-1 and LAMP-2, and the cell type-specific proteins DC-LAMP (LAMP-3), BAD-LAMP (UNC-46, C20orf103) and macrosialin (CD68). LAMPs have been implicated in a multitude of cellular processes, including phagocytosis, autophagy, lipid transport and aging. LAMP-2 isoform A acts as a receptor in chaperone-mediated autophagy. LAMP-2 deficiency causes the fatal Danon disease. The abundant proteins LAMP-1 and LAMP-2 are major constituents of the glycoconjugate coat present on the inside of the lysosomal membrane, the 'lysosomal glycocalyx'. The LAMP family is characterized by a conserved domain of 150 to 200 amino acids with two disulfide bonds. The crystal structure of the conserved domain of human DC-LAMP was solved. It is the first high-resolution structure of a heavily glycosylated lysosomal membrane protein. The structure represents a novel β-prism fold formed by two β-sheets bent by β-bulges and connected by a disulfide bond. Flexible loops and a hydrophobic pocket represent possible sites of molecular interaction. Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. The models correspond to the thickness of the lysosomal glycoprotein coat of only 5 to 12 nm, according to electron microscopy. The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown β-prism fold. Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
         datePublished:2012-07-19T00:00:00Z
         dateModified:2012-07-19T00:00:00Z
         pageStart:1
         pageEnd:15
         license:https://creativecommons.org/licenses/by/2.0
         sameAs:https://doi.org/10.1186/1741-7007-10-62
         keywords:
            Transmembrane Helix
            Lysosomal Membrane
            Late Endosome
            Luminal Domain
            Luminal Region
            Life Sciences
            general
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig2_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig3_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig4_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig5_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig6_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig7_HTML.jpg
         isPartOf:
            name:BMC Biology
            issn:
               1741-7007
            volumeNumber:10
            type:
               Periodical
               PublicationVolume
         publisher:
            name:BioMed Central
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Sonja Wilke
               affiliation:
                     name:Helmholtz Centre for Infection Research
                     address:
                        name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Joern Krausze
               affiliation:
                     name:Helmholtz Centre for Infection Research
                     address:
                        name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Konrad Büssow
               affiliation:
                     name:Helmholtz Centre for Infection Research
                     address:
                        name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx
      description:The family of lysosome-associated membrane proteins (LAMP) comprises the multifunctional, ubiquitous LAMP-1 and LAMP-2, and the cell type-specific proteins DC-LAMP (LAMP-3), BAD-LAMP (UNC-46, C20orf103) and macrosialin (CD68). LAMPs have been implicated in a multitude of cellular processes, including phagocytosis, autophagy, lipid transport and aging. LAMP-2 isoform A acts as a receptor in chaperone-mediated autophagy. LAMP-2 deficiency causes the fatal Danon disease. The abundant proteins LAMP-1 and LAMP-2 are major constituents of the glycoconjugate coat present on the inside of the lysosomal membrane, the 'lysosomal glycocalyx'. The LAMP family is characterized by a conserved domain of 150 to 200 amino acids with two disulfide bonds. The crystal structure of the conserved domain of human DC-LAMP was solved. It is the first high-resolution structure of a heavily glycosylated lysosomal membrane protein. The structure represents a novel β-prism fold formed by two β-sheets bent by β-bulges and connected by a disulfide bond. Flexible loops and a hydrophobic pocket represent possible sites of molecular interaction. Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. The models correspond to the thickness of the lysosomal glycoprotein coat of only 5 to 12 nm, according to electron microscopy. The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown β-prism fold. Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
      datePublished:2012-07-19T00:00:00Z
      dateModified:2012-07-19T00:00:00Z
      pageStart:1
      pageEnd:15
      license:https://creativecommons.org/licenses/by/2.0
      sameAs:https://doi.org/10.1186/1741-7007-10-62
      keywords:
         Transmembrane Helix
         Lysosomal Membrane
         Late Endosome
         Luminal Domain
         Luminal Region
         Life Sciences
         general
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig4_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig5_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig6_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1741-7007-10-62/MediaObjects/12915_2012_Article_577_Fig7_HTML.jpg
      isPartOf:
         name:BMC Biology
         issn:
            1741-7007
         volumeNumber:10
         type:
            Periodical
            PublicationVolume
      publisher:
         name:BioMed Central
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Sonja Wilke
            affiliation:
                  name:Helmholtz Centre for Infection Research
                  address:
                     name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Joern Krausze
            affiliation:
                  name:Helmholtz Centre for Infection Research
                  address:
                     name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Konrad Büssow
            affiliation:
                  name:Helmholtz Centre for Infection Research
                  address:
                     name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:BMC Biology
      issn:
         1741-7007
      volumeNumber:10
Organization:
      name:BioMed Central
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Helmholtz Centre for Infection Research
      address:
         name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
         type:PostalAddress
      name:Helmholtz Centre for Infection Research
      address:
         name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
         type:PostalAddress
      name:Helmholtz Centre for Infection Research
      address:
         name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Sonja Wilke
      affiliation:
            name:Helmholtz Centre for Infection Research
            address:
               name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
               type:PostalAddress
            type:Organization
      name:Joern Krausze
      affiliation:
            name:Helmholtz Centre for Infection Research
            address:
               name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
               type:PostalAddress
            type:Organization
      name:Konrad Büssow
      affiliation:
            name:Helmholtz Centre for Infection Research
            address:
               name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
      name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany
      name:Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany

External Links {🔗}(248)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Backbone.js
Clipboard.js
Prism.js

CDN Services {📦}

Crossref

5.68s.

LINK . SPRINGER . COM {}