Structural highlights
Function
S100G_BOVIN
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 cooperative binding of Ca2+ ions is an essential functional property of the EF-hand family of Ca2+-binding proteins. To understand how these proteins function, it is essential to characterize intermediate binding states in addition to the apo- and holo-proteins. The three-dimensional solution structure and fast time scale internal motional dynamics of the backbone have been determined for the half-saturated state of the N56A mutant of calbindin D9k with Ca2+ bound only in the N-terminal site. The extent of conformational reorganization and a loss of flexibility in the C-terminal EF-hand upon binding of an ion in the N-terminal EF-hand provide clear evidence of the importance of site-site interactions in this family of proteins, and demonstrates the strength of long-range effects in the cooperative EF-hand Ca2+-binding domain.
Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k.,Maler L, Blankenship J, Rance M, Chazin WJ Nat Struct Biol. 2000 Mar;7(3):245-50. PMID:10700285[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maler L, Blankenship J, Rance M, Chazin WJ. Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k. Nat Struct Biol. 2000 Mar;7(3):245-50. PMID:10700285 doi:10.1038/73369
