1vrk
From Proteopedia
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| - | [[Image:1vrk.gif|left|200px]]<br /><applet load="1vrk" size=" | + | [[Image:1vrk.gif|left|200px]]<br /><applet load="1vrk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vrk, resolution 1.90Å" /> | caption="1vrk, resolution 1.90Å" /> | ||
'''THE 1.9 ANGSTROM STRUCTURE OF E84K-CALMODULIN RS20 PEPTIDE COMPLEX'''<br /> | '''THE 1.9 ANGSTROM STRUCTURE OF E84K-CALMODULIN RS20 PEPTIDE COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] Known structural/functional Sites: <scene name='pdbsite=CA1:Ca Binding Site One'>CA1</scene>, <scene name='pdbsite=CA2:Ca Binding Site Two'>CA2</scene>, <scene name='pdbsite=CA3:Ca Binding Site Three'>CA3</scene> and <scene name='pdbsite=CA4:Ca Binding Site Four'>CA4</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=NH2:'>NH2</scene> 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] Known structural/functional Sites: <scene name='pdbsite=CA1:Ca+Binding+Site+One'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site+Two'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site+Three'>CA3</scene> and <scene name='pdbsite=CA4:Ca+Binding+Site+Four'>CA4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signalling]] | [[Category: signalling]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:17:06 2008'' |
Revision as of 08:17, 3 February 2008
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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 between E84K-CaM and RS20 peptide, the CaM recognition site, peptide from vertebrate smooth muscle and nonmuscle forms of myosin light, chain kinase, provides insight into the structural basis of the functional, communication between CaM's calcium ligation structures and protein, recognition surfaces. The structure reveals that the complex adapts to the, effect of the functional mutation by discrete adjustments in the helix, that contains E84. This helix is on the amino-terminal side of the, helix-loop-helix structural motif that is the first to be occupied in, CaM's calcium binding mechanism. The results reported here are consistent, with a sequential and cooperative model of CaM's calcium binding activity, in which the two globular and flexible central helix domains are, functionally linked, and provide insight into how CaM's calcium binding, activity and peptide recognition properties are functionally coupled.
About this Structure
1VRK is a Single protein structure of sequence from Synthetic construct with , and as ligands. Active as Transferred entry: 2.7.11.18, with EC number 2.7.1.117 Known structural/functional Sites: , , and . 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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