Structural highlights
Function
[PRVB_ESOLU] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.
X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.,Declercq JP, Tinant B, Parello J Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Declercq JP, Tinant B, Parello J. X-ray structure of a new crystal form of pike 4.10 beta parvalbumin. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738 doi:10.1107/S0907444995010006
