1avs

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{{STRUCTURE_1avs| PDB=1avs | SCENE= }}
{{STRUCTURE_1avs| PDB=1avs | SCENE= }}
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'''X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C'''
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===X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C===
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==Overview==
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We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.
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{{ABSTRACT_PUBMED_9367759}}
==About this Structure==
==About this Structure==
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[[Category: Muscle contraction]]
[[Category: Muscle contraction]]
[[Category: Troponin]]
[[Category: Troponin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:42:29 2008''

Revision as of 14:42, 30 June 2008

Image:1avs.png

Template:STRUCTURE 1avs

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

Template:ABSTRACT PUBMED 9367759

About this Structure

1AVS is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution., Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN, J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:9367759

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