1avs: Difference between revisions
New page: left|200px<br /><applet load="1avs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avs, resolution 1.75Å" /> '''X-RAY CRYSTALLOGRAPH... |
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[[Image:1avs.jpg|left|200px]]<br /><applet load="1avs" size=" | [[Image:1avs.jpg|left|200px]]<br /><applet load="1avs" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1avs, resolution 1.75Å" /> | caption="1avs, resolution 1.75Å" /> | ||
'''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== | ||
We have solved and refined the crystal and molecular structures of the | 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== | ||
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:// | 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]] | ||
[[Category: James, M | [[Category: James, M N.G.]] | ||
[[Category: Strynadka, N | [[Category: Strynadka, N C.J.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium-activated]] | [[Category: calcium-activated]] | ||
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[[Category: troponin]] | [[Category: troponin]] | ||
''Page seeded by [http:// | ''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
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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 CA 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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