1dmo: Difference between revisions
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[[Image:1dmo.gif|left|200px]] | [[Image:1dmo.gif|left|200px]] | ||
'''CALMODULIN, NMR, 30 STRUCTURES''' | {{Structure | ||
|PDB= 1dmo |SIZE=350|CAPTION= <scene name='initialview01'>1dmo</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]) | |||
}} | |||
'''CALMODULIN, NMR, 30 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DMO is a [ | 1DMO is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7552747 7552747] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: calcium-induced conformational change]] | [[Category: calcium-induced conformational change]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:53 2008'' | ||
Revision as of 08:40, 20 March 2008
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| Gene: | XENOPUS LAEVIS (Xenopus laevis) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Mar 20 10:40:53 2008
