1k96
From Proteopedia
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|PDB= 1k96 |SIZE=350|CAPTION= <scene name='initialview01'>1k96</scene>, resolution 1.44Å | |PDB= 1k96 |SIZE=350|CAPTION= <scene name='initialview01'>1k96</scene>, resolution 1.44Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k9p|1K9P]], [[1k8u|1K8U]], [[1k9k|1K9K]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k96 OCA], [http://www.ebi.ac.uk/pdbsum/1k96 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k96 RCSB]</span> | ||
}} | }} | ||
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[[Category: Dominguez, R.]] | [[Category: Dominguez, R.]] | ||
[[Category: Otterbein, L R.]] | [[Category: Otterbein, L R.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: CA]] | ||
[[Category: cacy]] | [[Category: cacy]] | ||
[[Category: calcium bound]] | [[Category: calcium bound]] | ||
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[[Category: s100a6]] | [[Category: s100a6]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:07 2008'' |
Revision as of 18:45, 30 March 2008
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| , resolution 1.44Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1K9P, 1K8U, 1K9K
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CALCIUM BOUND HUMAN S100A6
Overview
S100A6 is a member of the S100 family of Ca(2+) binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in the Ca(2+)-free and Ca(2+)-bound states to resolutions of 1.15 A and 1.44 A, respectively. Ca(2+) binding is responsible for a dramatic change in the global shape and charge distribution of the S100A6 dimer, leading to the exposure of two symmetrically positioned target binding sites. The results are consistent with S100A6, and most likely other S100 proteins, functioning as Ca(2+) sensors in a way analogous to the prototypical sensors calmodulin and troponin C. The structures have important implications for our understanding of target binding and cooperativity of Ca(2+) binding in the S100 family.
About this Structure
1K96 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution., Otterbein LR, Kordowska J, Witte-Hoffmann C, Wang CL, Dominguez R, Structure. 2002 Apr;10(4):557-67. PMID:11937060
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