1D1O
COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K
Summary for 1D1O
| Entry DOI | 10.2210/pdb1d1o/pdb |
| Related | 1CDN 1CLB 2BCB |
| NMR Information | BMRB: 4581 |
| Descriptor | CALBINDIN D9K (1 entity in total) |
| Functional Keywords | ef-hand, calcium-binding protein, signal transduction, signaling protein |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 8501.61 |
| Authors | Maler, L.,Blankenship, J.,Rance, M.,Chazin, W.J. (deposition date: 1999-09-20, release date: 2000-03-08, Last modification date: 2024-05-22) |
| Primary citation | Maler, L.,Blankenship, J.,Rance, M.,Chazin, W.J. Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k. Nat.Struct.Biol., 7:245-250, 2000 Cited by PubMed Abstract: 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. PubMed: 10700285DOI: 10.1038/73369 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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