1vrk

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(New page: 200px<br /> <applet load="1vrk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vrk, resolution 1.90&Aring;" /> '''THE 1.9 ANGSTROM ST...)
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==About this Structure==
==About this Structure==
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1VRK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]] with CA, ACT and NH2 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.117 2.7.1.117]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VRK OCA]].
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1VRK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]] with CA, ACT and NH2 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.18 Transferred entry: 2.7.11.18]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.117 2.7.1.117]]. Structure known Active Sites: CA1, CA2, CA3 and CA4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VRK OCA]].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
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[[Category: Transferred entry: 2.7.11.18]]
[[Category: Anderson, W.F.]]
[[Category: Anderson, W.F.]]
[[Category: Weigand, S.]]
[[Category: Weigand, S.]]
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[[Category: signalling]]
[[Category: signalling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:28:35 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:35:31 2007''

Revision as of 10:30, 30 October 2007


1vrk, resolution 1.90Å

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THE 1.9 ANGSTROM STRUCTURE OF E84K-CALMODULIN RS20 PEPTIDE COMPLEX

Overview

The enhancement of calmodulin's (CaM) calcium binding activity by an, enzyme or a recognition site peptide and its diminution by key point, mutations at the protein recognition interface (e.g., E84K-CaM), which is, more than 20 A away from the nearest calcium ligation structure, can be, described by an expanded version of the Adair-Klotz equation for, multiligand binding. The expanded equation can accurately describe the, calcium binding events and their variable linkage to protein recognition, events can be extended to other CaM-regulated enzymes and can potentially, be applied to a diverse array of ligand binding systems with allosteric, regulation of ligand binding, whether by other ligands or protein, interaction. The 1.9 A resolution X-ray crystallographic structure of the, complex ... [(full description)]

About this Structure

1VRK is a [Single protein] structure of sequence from [Synthetic construct] with CA, ACT and NH2 as [ligands]. Active as [Transferred entry: 2.7.11.18], with EC number [2.7.1.117]. Structure known Active Sites: CA1, CA2, CA3 and CA4. Full crystallographic information is available from [OCA].

Reference

Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties., Mirzoeva S, Weigand S, Lukas TJ, Shuvalova L, Anderson WF, Watterson DM, Biochemistry. 1999 Mar 30;38(13):3936-47. PMID:10194305

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