Structural highlights
Function
[NCALD_BOVIN] May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three 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
The crystal structure of calcium-bound unmyristoylated bovine neurocalcin from Escherichia coli has been determined at 2.4 A resolution. The three-dimensional structure reveals a highly compact structure consisting of: (i) two pairs of calcium-binding EF-hands (EF1-EF2 and EF3-EF4); (ii) a calcium ion bound at EF2, EF3 and EF4 sites; and (iii) an EF1-hand that is disabled from calcium-binding due to a Cys-Pro sequence in the Ca2+-binding loop. The crystal structure of neurocalcin resembles photoreceptor recoverin in overall topology, however its EF2- and EF4-hands differ. Recently, neurocalcin in the calcium-bound state has been shown to stimulate mammalian rod outer segment membrane guanylate cyclase. A possible site for cyclase activity based on the three-dimensional structure is discussed.
Crystal structure of recombinant bovine neurocalcin.,Vijay-Kumar S, Kumar VD Nat Struct Biol. 1999 Jan;6(1):80-8. PMID:9886296[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vijay-Kumar S, Kumar VD. Crystal structure of recombinant bovine neurocalcin. Nat Struct Biol. 1999 Jan;6(1):80-8. PMID:9886296 doi:10.1038/4956
