1deg: Difference between revisions

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-[[Image:1deg.gif|left|200px]]
+{{Seed}}
+[[Image:1deg.png|left|200px]]
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 {{STRUCTURE_1deg|  PDB=1deg  |  SCENE=  }}
-'''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.
+-->
+{{ABSTRACT_PUBMED_8341712}}
 ==About this Structure==
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 [[Category: Sobottk, S E.]]
 [[Category: Calcium-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:45:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:54:09 2008''