2fwu
From Proteopedia
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|PDB= 2fwu |SIZE=350|CAPTION= <scene name='initialview01'>2fwu</scene> | |PDB= 2fwu |SIZE=350|CAPTION= <scene name='initialview01'>2fwu</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NCX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | |GENE= NCX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fws|2FWS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fwu OCA], [http://www.ebi.ac.uk/pdbsum/2fwu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fwu RCSB]</span> | ||
}} | }} | ||
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[[Category: Hilge, M.]] | [[Category: Hilge, M.]] | ||
[[Category: Vuister, G W.]] | [[Category: Vuister, G W.]] | ||
| - | [[Category: CA]] | ||
[[Category: beta-bulge]] | [[Category: beta-bulge]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
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[[Category: greek key]] | [[Category: greek key]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:08:45 2008'' |
Revision as of 00:08, 31 March 2008
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| Ligands: | |||||||
| Gene: | NCX1 (Canis lupus familiaris) | ||||||
| Related: | 2FWS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Second Ca2+ binding domain of the Na,Ca-exchanger (NCX1)
Overview
The plasma membrane Na+/Ca2+ exchanger (NCX) is almost certainly the major Ca2+ extrusion mechanism in cardiac myocytes. Binding of Na+ and Ca2+ ions to its large cytosolic loop regulates ion transport of the exchanger. We determined the solution structures of two Ca2+ binding domains (CBD1 and CBD2) that, together with an alpha-catenin-like domain (CLD), form the regulatory exchanger loop. CBD1 and CBD2 are very similar in the Ca2+ bound state and describe the Calx-beta motif. Strikingly, in the absence of Ca2+, the upper half of CBD1 unfolds while CBD2 maintains its structural integrity. Together with a 7-fold higher affinity for Ca2+, this suggests that CBD1 is the primary Ca2+ sensor. Specific point mutations in either domain largely allow the interchange of their functionality and uncover the mechanism underlying Ca2+ sensing in NCX.
About this Structure
2FWU is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
Reference
Ca2+ regulation in the Na+/Ca2+ exchanger involves two markedly different Ca2+ sensors., Hilge M, Aelen J, Vuister GW, Mol Cell. 2006 Apr 7;22(1):15-25. PMID:16600866
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