1deg: Difference between revisions

Revision as of 22:54, 30 June 2008

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File:1deg.png

Template:STRUCTURE 1deg

THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURETHE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

Template:ABSTRACT PUBMED 8341712

About this StructureAbout this Structure

1DEG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

The linker of des-Glu84-calmodulin is bent., Raghunathan S, Chandross RJ, Cheng BP, Persechini A, Sobottka SE, Kretsinger RH, Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6869-73. PMID:8341712

Page seeded by OCA on Mon Jun 30 22:54:09 2008

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OCA

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-'''THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE'''
+===THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE===
-==Overview==
+<!--
-The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.
+The line below this paragraph, {{ABSTRACT_PUBMED_8341712}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8341712 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8341712}}
 ==About this Structure==
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 [[Category: Sobottk, S E.]]
 [[Category: Calcium-binding protein]]
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