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 1.90Å" /> '''THE 1.9 ANGSTROM ST...)
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Revision as of 17:23, 29 October 2007
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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 [[1]], with EC number [2.7.1.117]. 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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