2FWS
First Ca2+ binding domain of the Na,Ca-exchanger (NCX1)
Summary for 2FWS
| Entry DOI | 10.2210/pdb2fws/pdb |
| Related | 2fwu |
| NMR Information | BMRB: 7009 |
| Descriptor | Sodium/calcium exchanger 1, CALCIUM ION (2 entities in total) |
| Functional Keywords | beta-sandwich, greek key, cis-proline, beta-bulge, ca2+ binding, metal transport regulator |
| Biological source | Canis lupus familiaris (dog) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P23685 |
| Total number of polymer chains | 1 |
| Total formula weight | 15243.67 |
| Authors | Hilge, M.,Aelen, J.,Vuister, G.W. (deposition date: 2006-02-03, release date: 2006-04-18, Last modification date: 2024-05-29) |
| Primary citation | Hilge, M.,Aelen, J.,Vuister, G.W. Ca(2+) regulation in the na(+)/ca(2+) exchanger involves two markedly different ca(2+) sensors Mol.Cell, 22:15-25, 2006 Cited by PubMed Abstract: 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. PubMed: 16600866DOI: 10.1016/j.molcel.2006.03.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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