1d1o: Difference between revisions
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'''COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K''' | {{Structure | ||
|PDB= 1d1o |SIZE=350|CAPTION= <scene name='initialview01'>1d1o</scene> | |||
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'''COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1D1O is a [ | 1D1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1O OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10700285 10700285] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:31:40 2008'' | ||
Revision as of 08:31, 20 March 2008
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COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K
Overview
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.
About this Structure
1D1O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
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