1w15
From Proteopedia
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- | [[Image:1w15.gif|left|200px]] | + | [[Image:1w15.gif|left|200px]] |
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- | '''RAT SYNAPTOTAGMIN 4 C2B DOMAIN IN THE PRESENCE OF CALCIUM''' | + | {{Structure |
+ | |PDB= 1w15 |SIZE=350|CAPTION= <scene name='initialview01'>1w15</scene>, resolution 1.93Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''RAT SYNAPTOTAGMIN 4 C2B DOMAIN IN THE PRESENCE OF CALCIUM''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1W15 is a [ | + | 1W15 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W15 OCA]. |
==Reference== | ==Reference== | ||
- | Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4., Dai H, Shin OH, Machius M, Tomchick DR, Sudhof TC, Rizo J, Nat Struct Mol Biol. 2004 Sep;11(9):844-9. Epub 2004 Aug 15. PMID:[http:// | + | Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4., Dai H, Shin OH, Machius M, Tomchick DR, Sudhof TC, Rizo J, Nat Struct Mol Biol. 2004 Sep;11(9):844-9. Epub 2004 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15311271 15311271] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:37 2008'' |
Revision as of 12:50, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
RAT SYNAPTOTAGMIN 4 C2B DOMAIN IN THE PRESENCE OF CALCIUM
Overview
The neuronal protein synaptotagmin 1 functions as a Ca(2+) sensor in exocytosis via two Ca(2+)-binding C(2) domains. The very similar synaptotagmin 4, which includes all the predicted Ca(2+)-binding residues in the C(2)B domain but not in the C(2)A domain, is also thought to function as a neuronal Ca(2+) sensor. Here we show that, unexpectedly, both C(2) domains of fly synaptotagmin 4 exhibit Ca(2+)-dependent phospholipid binding, whereas neither C(2) domain of rat synaptotagmin 4 binds Ca(2+) or phospholipids efficiently. Crystallography reveals that changes in the orientations of critical Ca(2+) ligands, and perhaps their flexibility, render the rat synaptotagmin 4 C(2)B domain unable to form full Ca(2+)-binding sites. These results indicate that synaptotagmin 4 is a Ca(2+) sensor in the fly but not in the rat, that the Ca(2+)-binding properties of C(2) domains cannot be reliably predicted from sequence analyses, and that proteins clearly identified as orthologs may nevertheless have markedly different functional properties.
About this Structure
1W15 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4., Dai H, Shin OH, Machius M, Tomchick DR, Sudhof TC, Rizo J, Nat Struct Mol Biol. 2004 Sep;11(9):844-9. Epub 2004 Aug 15. PMID:15311271
Page seeded by OCA on Thu Mar 20 14:50:37 2008
Categories: Rattus norvegicus | Single protein | Dai, H. | Machius, M. | Rizo, J. | Shin, O H. | Sudhof, T C. | Tomchick, D R. | CA | CL | NA | Calcium | Endocytosis/exocytosis | Neurotransmitter release | Synaptotagmin | Transmembrane