1dmo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1dmo.gif|left|200px]]
[[Image:1dmo.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1dmo |SIZE=350|CAPTION= <scene name='initialview01'>1dmo</scene>
+
The line below this paragraph, containing "STRUCTURE_1dmo", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1dmo| PDB=1dmo | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmo OCA], [http://www.ebi.ac.uk/pdbsum/1dmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dmo RCSB]</span>
+
-
}}
+
'''CALMODULIN, NMR, 30 STRUCTURES'''
'''CALMODULIN, NMR, 30 STRUCTURES'''
Line 28: Line 25:
[[Category: Tanaka, T.]]
[[Category: Tanaka, T.]]
[[Category: Zhang, M.]]
[[Category: Zhang, M.]]
-
[[Category: calcium-binding protein]]
+
[[Category: Calcium-binding protein]]
-
[[Category: calcium-induced conformational change]]
+
[[Category: Calcium-induced conformational change]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:01:49 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:48 2008''
+

Revision as of 11:01, 2 May 2008

Image:1dmo.gif

Template:STRUCTURE 1dmo

CALMODULIN, NMR, 30 STRUCTURES


Overview

The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.

About this Structure

1DMO is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

Calcium-induced conformational transition revealed by the solution structure of apo calmodulin., Zhang M, Tanaka T, Ikura M, Nat Struct Biol. 1995 Sep;2(9):758-67. PMID:7552747 Page seeded by OCA on Fri May 2 14:01:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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