Parvalbumin: Difference between revisions
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<StructureSection load='2pvb' size='350' side='right' caption='Pike parvalbumin complex with Ca+2 ions (green), ammonium, acetyl and formate (PDB entry [[2pvb]])' scene=''> | <StructureSection load='2pvb' size='350' side='right' caption='Pike parvalbumin complex with Ca+2 ions (green), ammonium, acetyl and formate (PDB entry [[2pvb]])' scene=''> | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
PVA contains a heptacoordinated Ca+2 ion binding to 7 oxygen atoms in a typical EF-hand coordination<ref>PMID:10548066</ref>. | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Parvalbumin == | == 3D Structures of Parvalbumin == | ||
Revision as of 11:25, 15 June 2016
FunctionParvalbumin (PVA) is a calcium-binding albumin protein. PVA is involved in calcium signaling[1]. PVA contains 3 domains: AB, CD (N-terminal) and EF (C-terminal). See also Structural highlightsPVA contains a heptacoordinated Ca+2 ion binding to 7 oxygen atoms in a typical EF-hand coordination[2]. |
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3D Structures of Parvalbumin3D Structures of Parvalbumin
Updated on 15-June-2016
ReferencesReferences
- ↑ Cates MS, Teodoro ML, Phillips GN Jr. Molecular mechanisms of calcium and magnesium binding to parvalbumin. Biophys J. 2002 Mar;82(3):1133-46. PMID:11867433 doi:http://dx.doi.org/10.1016/S0006-3495(02)75472-6
- ↑ Declercq JP, Evrard C, Lamzin V, Parello J. Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core. Protein Sci. 1999 Oct;8(10):2194-204. PMID:10548066