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2i1y

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Structural genomics of protein phosphatases. J.STRUCT.FUNCT.GENOM. 8 121-140 2007
    Site NYSGXRC
    PDB Id 2i1y Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS7907,PF00102, NP_002837
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.23 Rfactor 0.19907
    Waters
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    Solvent Content 48.56

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    Ligand Information
    Ligands GOL (GLYCEROL) x 2
    Metals

    Jmol

     
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    Google Scholar output for 2i1y
    1. Structural genomics of protein phosphatases
    SC Almo, JB Bonanno, JM Sauder, S Emtage - Journal of structural and , 2007 - Springer
     

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    Protein Summary

    IA-2 is a receptor-type protein tyrosine phosphatase. The full length protein is enriched in the secretory granules of neuroendocrine cells, including pancreatic islet B cells, peptidergic neurons, pituitary cells, and adrenal chromaffin cells. The protein appears to lack phosphatase activity, but its localization to the membrane of insulin secretory granules suggests that it may be involved in granule trafficking and/or maturation. IA-2-deficient mice exhibit defects in glucose-stimulated insulin secretion. The protein is a major autoantigen in type 1 diabetes; over 50% of patients demonstrate antibodies to IA-2.
    The structure is similar to PTP1B, but several residues critical for activity are absent, including the catalytic acid in the WPD loop (Ala instead of Asp) and a major determinant (Tyr) in the phosphotyrosine-recognition loop. It is known to heterodimerize with both PTPalpha and PTPepsilon and can down-regulate the activity of PTPalpha, since it is catalytically inactive.


    Ligand Summary

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