1avs

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(New page: 200px<br /><applet load="1avs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avs, resolution 1.75&Aring;" /> '''X-RAY CRYSTALLOGRAPH...)
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[[Image:1avs.jpg|left|200px]]<br /><applet load="1avs" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1avs, resolution 1.75&Aring;" />
caption="1avs, resolution 1.75&Aring;" />
'''X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C'''<br />
'''X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1AVS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVS OCA].
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1AVS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVS OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: James, M.N.G.]]
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[[Category: James, M N.G.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-activated]]
[[Category: calcium-activated]]
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[[Category: troponin]]
[[Category: troponin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:09:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:46 2008''

Revision as of 09:48, 21 February 2008


1avs, resolution 1.75Å

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

Overview

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.

About this Structure

1AVS is a Single protein structure of sequence from Gallus gallus with as ligand. 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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