We are analyzing https://link.springer.com/article/10.1007/s12013-018-0854-5.

Title:
Biophysical Characterization of SG2NA Variants and their Interaction with DJ-1 and Calmodulin in vitro | Cell Biochemistry and Biophysics
Description:
SG2NA was first discovered as nuclear autoantigen in lung and bladder cancer patient. It was named SG2NA as its expression increases during S to G2 phase of cell cycle. SG2NA/Striatin3 was classified as a member of Striatin family along with Straitin and Zinedin due to its structural and functional relatedness. At the molecular level, SG2NA is characterized by the presence of multiple protein–protein interaction domains viz., a caveolin binding motif, a coiled coil structure, Ca2+—calmodulin binding domain and a large WD-40 repeat domain in the same order from amino to the carboxyl termini. Analysis of secondary structures of 87 and 78 kDa SG2NA isoforms showed characteristic combinations of α-helix, β-structure, β-turns and random coil; suggesting of effective refolding after denaturation. This study for the first time establishes the structural differences between the two prevalent isoforms of SG2NA. Recently we observed that DJ-1 interacts with variants of SG2NA both in vitro and in vivo. The SG2NA isoforms purified from inclusion bodies showed the different secondary structure conformations, stability and interaction pattern for their interacting partners (DJ-1 and calmodulin) which imparts functional diversity of SG2NA. The SG2NA isoforms showed significant differential binding affinity to DJ-1 and Calmodulin.
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Keywords {🔍}

article, google, scholar, cas, pubmed, sgna, protein, journal, cell, goswami, proteins, research, jain, striatin, family, central, interaction, analysis, variants, calmodulin, soni, structure, repeat, isoforms, access, india, privacy, cookies, content, binding, domain, biological, chemistry, tanti, biology, publish, search, biophysical, sangeeta, buddhi, prakash, nuclear, autoantigen, expression, structural, molecular, secondary, differential, castets, calmodulinbinding,

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ca2+—calmodulin binding domain month download article/chapter protein-protein interaction cell-cycle nuclear autoantigen experimental cell research bmc research notes secondary structure conformations immunoprecipitation-western blot analysis karunakar kar narrow active-site cleft article cell biochemistry sneha sudha komath & shyamal calmodulin-binding proteins dna-binding nuclear autoantigen core stripak proteins protein phosphatase 2a calmodulin-binding protein full article pdf disease protein dj-1 parkinsonism protein dj-1 scaffold protein sg2na buddhi prakash jain privacy choices/manage cookies coiled coil structure striatin-interacting phosphatase structure-function analysis sneha sudha komath wd-40 motifs expressed sg2na protein variants multiple splice variants armadillo repeat domain check access instant access article soni related subjects biophysical research communications sg2na isoforms purified inclusion bodies showed wd-repeat family cell cycle caveolin binding motif comparative binding mechanism α-1-acid glycoprotein profile sg2na recruits dj-1 bladder cancer patient jawaharlal nehru university coiled-coil domain european economic area growth responsive properties

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WD40 repeat domain proteins: a novel target class?

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         description:SG2NA was first discovered as nuclear autoantigen in lung and bladder cancer patient. It was named SG2NA as its expression increases during S to G2 phase of cell cycle. SG2NA/Striatin3 was classified as a member of Striatin family along with Straitin and Zinedin due to its structural and functional relatedness. At the molecular level, SG2NA is characterized by the presence of multiple protein–protein interaction domains viz., a caveolin binding motif, a coiled coil structure, Ca2+—calmodulin binding domain and a large WD-40 repeat domain in the same order from amino to the carboxyl termini. Analysis of secondary structures of 87 and 78 kDa SG2NA isoforms showed characteristic combinations of α-helix, β-structure, β-turns and random coil; suggesting of effective refolding after denaturation. This study for the first time establishes the structural differences between the two prevalent isoforms of SG2NA. Recently we observed that DJ-1 interacts with variants of SG2NA both in vitro and in vivo. The SG2NA isoforms purified from inclusion bodies showed the different secondary structure conformations, stability and interaction pattern for their interacting partners (DJ-1 and calmodulin) which imparts functional diversity of SG2NA. The SG2NA isoforms showed significant differential binding affinity to DJ-1 and Calmodulin.
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      headline:Biophysical Characterization of SG2NA Variants and their Interaction with DJ-1 and Calmodulin in vitro
      description:SG2NA was first discovered as nuclear autoantigen in lung and bladder cancer patient. It was named SG2NA as its expression increases during S to G2 phase of cell cycle. SG2NA/Striatin3 was classified as a member of Striatin family along with Straitin and Zinedin due to its structural and functional relatedness. At the molecular level, SG2NA is characterized by the presence of multiple protein–protein interaction domains viz., a caveolin binding motif, a coiled coil structure, Ca2+—calmodulin binding domain and a large WD-40 repeat domain in the same order from amino to the carboxyl termini. Analysis of secondary structures of 87 and 78 kDa SG2NA isoforms showed characteristic combinations of α-helix, β-structure, β-turns and random coil; suggesting of effective refolding after denaturation. This study for the first time establishes the structural differences between the two prevalent isoforms of SG2NA. Recently we observed that DJ-1 interacts with variants of SG2NA both in vitro and in vivo. The SG2NA isoforms purified from inclusion bodies showed the different secondary structure conformations, stability and interaction pattern for their interacting partners (DJ-1 and calmodulin) which imparts functional diversity of SG2NA. The SG2NA isoforms showed significant differential binding affinity to DJ-1 and Calmodulin.
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         Biological and Medical Physics
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