Parvalbumin: Difference between revisions
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<StructureSection load='2pvb' size=' | <StructureSection load='2pvb' size='350' side='right' caption='Pike parvalbumin complex with Ca+2 ions (green), ammonium ion (blue), acetyl and formate (PDB entry [[2pvb]])' scene='46/466520/Cv/2' pspeed='8'> | ||
== Function == | == Function == | ||
'''Parvalbumin (PVA)''' is a calcium-binding albumin protein. PVA is involved in calcium signaling<ref>PMID:11867433</ref>. PVA contains 3 domains each containing 2 helices: AB, CD (N-terminal) and EF (C-terminal). '''α-parvalbumin''' differs from '''β-parvalbumin''' in 54 positions. α-parvalbumin is expressed in various tissues while β-parvalbumin is expressed only in preterm placenta<ref>PMID:8354278</ref>. <br /> | '''Parvalbumin (PVA)''' is a calcium-binding albumin protein. PVA is involved in calcium signaling<ref>PMID:11867433</ref>. PVA contains 3 domains each containing 2 helices: AB, CD (N-terminal) and EF (C-terminal). '''α-parvalbumin''' differs from '''β-parvalbumin''' in 54 positions. α-parvalbumin is expressed in various tissues while β-parvalbumin is expressed only in preterm placenta<ref>PMID:8354278</ref>. <br /> | ||
Revision as of 14:10, 15 August 2018
FunctionParvalbumin (PVA) is a calcium-binding albumin protein. PVA is involved in calcium signaling[1]. PVA contains 3 domains each containing 2 helices: AB, CD (N-terminal) and EF (C-terminal). α-parvalbumin differs from β-parvalbumin in 54 positions. α-parvalbumin is expressed in various tissues while β-parvalbumin is expressed only in preterm placenta[2]. See also RelevancePVA is a major fish allergen[3]. Structural highlightsPVA contains a in a coordination[4]. .
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3D Structures of Parvalbumin3D Structures of Parvalbumin
Updated on 15-August-2018
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
- ↑ Fohr UG, Weber BR, Muntener M, Staudenmann W, Hughes GJ, Frutiger S, Banville D, Schafer BW, Heizmann CW. Human alpha and beta parvalbumins. Structure and tissue-specific expression. Eur J Biochem. 1993 Aug 1;215(3):719-27. PMID:8354278
- ↑ Lim DL, Neo KH, Yi FC, Chua KY, Goh DL, Shek LP, Giam YC, Van Bever HP, Lee BW. Parvalbumin--the major tropical fish allergen. Pediatr Allergy Immunol. 2008 Aug;19(5):399-407. doi:, 10.1111/j.1399-3038.2007.00674.x. Epub 2008 Jan 25. PMID:18221468 doi:http://dx.doi.org/10.1111/j.1399-3038.2007.00674.x
- ↑ 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