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...) |
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| - | [[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== | ||
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[[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
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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
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