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 1.9&Aring;" /> '''STRUCTURE OF THE FIRS...)
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[[Image:1rsy.gif|left|200px]]<br /><applet load="1rsy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rsy, resolution 1.9&Aring;" />
caption="1rsy, resolution 1.9&Aring;" />
'''STRUCTURE OF THE FIRST C2-DOMAIN OF SYNAPTOTAGMIN I: A NOVEL CA2+(SLASH)PHOSPHOLIPID BINDING FOLD'''<br />
'''STRUCTURE OF THE FIRST C2-DOMAIN OF SYNAPTOTAGMIN I: A NOVEL CA2+(SLASH)PHOSPHOLIPID BINDING FOLD'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1RSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RSY OCA].
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1RSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSY OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sprang, S.R.]]
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[[Category: Sprang, S R.]]
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[[Category: Sutton, R.B.]]
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[[Category: Sutton, R B.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: calcium/phospholipid binding protein]]
[[Category: calcium/phospholipid binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:51:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:09 2008''

Revision as of 12:54, 21 February 2008


1rsy, resolution 1.9Å

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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 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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