Structural highlights
Function
[PRVA_HUMAN] 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
In the frame of a research aimed at the detailed structural characterization of human calcium-binding proteins of the EF-hand family, the solution structure of human alpha-parvalbumin has been solved by NMR and refined with the help of substitution of the Ca(2+) ion in the EF site with the paramagnetic Dy(3+) ion. A simple (1)H-(15)N HSQC spectrum allowed the NH assignments based on the properties of Dy(3+). This allowed us to exploit pseudocontact shifts and residual dipolar couplings for solution structure refinement. The backbone and heavy atom RMSD are 0.55 +/- 0.08 and 1.02 +/- 0.08 A, respectively, and decrease to 0.39 +/- 0.05 and 0.90 +/- 0.06 A upon refinement with paramagnetism-based restraints. The RMSD for the metal itself in the EF site in the refined structure is 0.26 +/- 0.12 A. Backbone NH R(1), R(2), and NOE measured at two temperatures show the protein to be relatively rigid. The NH orientations are well determined by the paramagnetism-based restraints. This allows us to detect small but significant local structural differences with the orthologue protein from rat, whose X-ray structure is available at 2.0 A resolution. All differences are related to local changes in the amino acidic composition.
Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin.,Baig I, Bertini I, Del Bianco C, Gupta YK, Lee YM, Luchinat C, Quattrone A Biochemistry. 2004 May 11;43(18):5562-73. PMID:15122922[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baig I, Bertini I, Del Bianco C, Gupta YK, Lee YM, Luchinat C, Quattrone A. Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin. Biochemistry. 2004 May 11;43(18):5562-73. PMID:15122922 doi:10.1021/bi035879k