1dmo

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[[Image:1dmo.gif|left|200px]]
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{{STRUCTURE_1dmo| PDB=1dmo | SCENE= }}
{{STRUCTURE_1dmo| PDB=1dmo | SCENE= }}
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'''CALMODULIN, NMR, 30 STRUCTURES'''
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===CALMODULIN, NMR, 30 STRUCTURES===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7552747 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7552747}}
==About this Structure==
==About this Structure==
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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].
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1DMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA].
==Reference==
==Reference==
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[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
[[Category: Calcium-induced conformational change]]
[[Category: Calcium-induced conformational change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:01:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:18:22 2008''

Revision as of 20:18, 30 June 2008

Template:STRUCTURE 1dmo

CALMODULIN, NMR, 30 STRUCTURES

Template:ABSTRACT PUBMED 7552747

About this Structure

1DMO is a Single protein structure of sequence from Xenopus laevis. Full experimental 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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