We are analyzing https://link.springer.com/article/10.1007/s12104-015-9609-z.

Title:
Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3 | Biomolecular NMR Assignments
Description:
Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.
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Keywords {🔍}

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Topics {✒️}

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Schema {🗺️}

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         headline:Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3
         description:Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.
         datePublished:2015-04-19T00:00:00Z
         dateModified:2015-04-19T00:00:00Z
         pageStart:355
         pageEnd:358
         sameAs:https://doi.org/10.1007/s12104-015-9609-z
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            SNX3
            PX domain
            Phosphoinositide recognition
            Phosphatidylinositol 3-phosphate
            Endosome
            NMR
            Biological and Medical Physics
            Biophysics
            Polymer Sciences
            Biochemistry
            general
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      headline:Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3
      description:Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.
      datePublished:2015-04-19T00:00:00Z
      dateModified:2015-04-19T00:00:00Z
      pageStart:355
      pageEnd:358
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         SNX3
         PX domain
         Phosphoinositide recognition
         Phosphatidylinositol 3-phosphate
         Endosome
         NMR
         Biological and Medical Physics
         Biophysics
         Polymer Sciences
         Biochemistry
         general
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            type:Person
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                  name:University of Geneva
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            affiliation:
                  name:University of Birmingham
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               type:PostalAddress
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      affiliation:
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            address:
               name:Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Birmingham, UK
               type:PostalAddress
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      name:Jean Gruenberg
      affiliation:
            name:University of Geneva
            address:
               name:Department of Biochemistry Sciences II, University of Geneva, Geneva 4, Switzerland
               type:PostalAddress
            type:Organization
      name:Marc Lenoir
      affiliation:
            name:University of Birmingham
            address:
               name:Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Birmingham, UK
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      name:Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Birmingham, UK
      name:Department of Biochemistry Sciences II, University of Geneva, Geneva 4, Switzerland
      name:Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Birmingham, UK

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