1bhd: Difference between revisions
New page: left|200px<br /> <applet load="1bhd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhd, resolution 2.0Å" /> '''SECOND CALPONIN HOMO... |
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'''SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN'''<br /> | '''SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN'''<br /> | ||
==Overview== | ==Overview== | ||
Utrophin is a close homologue of dystrophin, the protein defective in | 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. | ||
==About this Structure== | ==About this Structure== | ||
1BHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1BHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Keep, N | [[Category: Keep, N H.]] | ||
[[Category: Kendrick-Jones, J.]] | [[Category: Kendrick-Jones, J.]] | ||
[[Category: Winder, S | [[Category: Winder, S J.]] | ||
[[Category: actin binding]] | [[Category: actin binding]] | ||
[[Category: calponin homology]] | [[Category: calponin homology]] | ||
[[Category: structural protein]] | [[Category: structural protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:19 2008'' | ||
Revision as of 12:55, 21 February 2008
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SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN
OverviewOverview
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.
About this StructureAbout this Structure
1BHD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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