1rsy
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(New page: 200px<br /><applet load="1rsy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rsy, resolution 1.9Å" /> '''STRUCTURE OF THE FIRS...)
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Revision as of 23:43, 20 November 2007
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STRUCTURE OF THE FIRST C2-DOMAIN OF SYNAPTOTAGMIN I: A NOVEL CA2+(SLASH)PHOSPHOLIPID BINDING FOLD
Overview
C2 domains are regulatory sequence motifs that occur widely in nature., Synaptotagmin I, a synaptic vesicle protein involved in the Ca2+, regulation of exocytosis, contains two C2 domains, the first of which acts, as a Ca2+ sensor. We now describe the three-dimensional structure of this, C2 domain at 1.9 A resolution in both the Ca(2+)-bound and Ca(2+)-free, forms. The C2 polypeptide forms an eight-stranded beta sandwich, constructed around a conserved four-stranded motif designated as a C2 key., Ca2+ binds in a cup-shaped depression between two polypeptide loops, located at the N- and C-termini of the C2-key motif.
About this Structure
1RSY is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold., Sutton RB, Davletov BA, Berghuis AM, Sudhof TC, Sprang SR, Cell. 1995 Mar 24;80(6):929-38. PMID:7697723
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