1d1o

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(New page: 200px<br /><applet load="1d1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1o" /> '''COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEI...)
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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'''<br />
'''COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1D1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D1O OCA].
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1D1O is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Blankenship, J.]]
[[Category: Blankenship, J.]]
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[[Category: Chazin, W.J.]]
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[[Category: Chazin, W J.]]
[[Category: Maler, L.]]
[[Category: Maler, L.]]
[[Category: Rance, M.]]
[[Category: Rance, M.]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:56:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:02 2008''

Revision as of 10:12, 21 February 2008


1d1o

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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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