This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dmo
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1dmo.gif|left|200px]] | [[Image:1dmo.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1dmo", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1dmo| PDB=1dmo | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''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: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 11:01, 2 May 2008
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
