We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1exr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1exr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1exr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1exr| PDB=1exr | SCENE= }}
{{STRUCTURE_1exr| PDB=1exr | SCENE= }}
-
'''THE 1.0 ANGSTROM CRYSTAL STRUCTURE OF CA+2 BOUND CALMODULIN'''
+
===THE 1.0 ANGSTROM CRYSTAL STRUCTURE OF CA+2 BOUND CALMODULIN===
-
==Overview==
+
<!--
-
Calmodulin (CaM) is a highly conserved 17 kDa eukaryotic protein that can bind specifically to over 100 protein targets in response to a Ca(2+) signal. Ca(2+)-CaM requires a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain poorly characterized. Here, we present the 1.0 A crystal structure of Paramecium tetraurelia Ca(2+)-CaM, including 36 discretely disordered residues and a fifth Ca(2+) that mediates a crystal contact. The 36 discretely disordered residues are located primarily in the central helix and the two hydrophobic binding pockets, and reveal correlated side-chain disorder that may assist target-specific deformation of the binding pockets. Evidence of domain displacements and discrete backbone disorder is provided by translation-libration-screw (TLS) analysis and multiconformer models of protein disorder, respectively. In total, the evidence for disorder at every accessible length-scale in Ca(2+)-CaM suggests that the protein occupies a large number of hierarchically arranged conformational substates in the crystalline environment and may sample a quasi-continuous spectrum of conformations in solution. Therefore, we propose that the functionally distinct forms of CaM are less structurally distinct than previously believed, and that the different activities of CaM in response to Ca(2+) may result primarily from Ca(2+)-mediated alterations in the dynamics of the protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10966818}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10966818 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10966818}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Disorder]]
[[Category: Disorder]]
[[Category: High resolution]]
[[Category: High resolution]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:38:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:10:57 2008''

Revision as of 23:10, 30 June 2008

Image:1exr.png

Template:STRUCTURE 1exr

THE 1.0 ANGSTROM CRYSTAL STRUCTURE OF CA+2 BOUND CALMODULIN

Template:ABSTRACT PUBMED 10966818

About this Structure

1EXR is a Single protein structure of sequence from Paramecium tetraurelia. Full crystallographic information is available from OCA.

Reference

The 1.0 A crystal structure of Ca(2+)-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity., Wilson MA, Brunger AT, J Mol Biol. 2000 Sep 1;301(5):1237-56. PMID:10966818

Page seeded by OCA on Tue Jul 1 02:10:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1exr"
Personal tools