Parvalbumin

From Proteopedia

spinqualitylabelsall models Pike parvalbumin complex with Ca+2 ions (green), ammonium ion (blue), acetyl and formate (PDB entry 2pvb) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Parvalbumin (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 EF hand Parvalbumin carp. Relevance PVA is a major fish allergen[3]. Structural highlights PVA contains a in a coordination[4]. Water molecules are shown as red spheres. . .

3D Structures of Parvalbumin

Updated on 05-December-2021

References

1. ↑ 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
2. ↑ 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
3. ↑ 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
4. ↑ 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