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
(New page: 200px<br /><applet load="1dmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmo" /> '''CALMODULIN, NMR, 30 STRUCTURES'''<br /> ==O...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dmo.gif|left|200px]]<br /><applet load="1dmo" size=" | + | [[Image:1dmo.gif|left|200px]]<br /><applet load="1dmo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dmo" /> | caption="1dmo" /> | ||
'''CALMODULIN, NMR, 30 STRUCTURES'''<br /> | '''CALMODULIN, NMR, 30 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of Ca(2+)-free calmodulin has been determined by | + | 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== | ==About this Structure== | ||
| - | 1DMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http:// | + | 1DMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: calcium-induced conformational change]] | [[Category: calcium-induced conformational change]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:15 2008'' |
Revision as of 10:18, 21 February 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 Thu Feb 21 12:18:15 2008
