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1bhd

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[[Image:1bhd.gif|left|200px]]
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{{STRUCTURE_1bhd| PDB=1bhd | SCENE= }}
{{STRUCTURE_1bhd| PDB=1bhd | SCENE= }}
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'''SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN'''
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===SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN===
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==Overview==
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Utrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin.
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The line below this paragraph, {{ABSTRACT_PUBMED_9887274}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9887274 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9887274}}
==About this Structure==
==About this Structure==
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[[Category: Calponin homology]]
[[Category: Calponin homology]]
[[Category: Structural protein]]
[[Category: Structural protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:30:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:12 2008''

Revision as of 16:10, 30 June 2008

Template:STRUCTURE 1bhd

SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN

Template:ABSTRACT PUBMED 9887274

About this Structure

1BHD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin., Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J, J Mol Biol. 1999 Jan 22;285(3):1257-64. PMID:9887274

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