1qag: Difference between revisions
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New page: left|200px<br /> <applet load="1qag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qag, resolution 3.00Å" /> '''Actin binding regio... |
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[[Image:1qag.gif|left|200px]]<br /> | [[Image:1qag.gif|left|200px]]<br /><applet load="1qag" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1qag" size=" | |||
caption="1qag, resolution 3.00Å" /> | caption="1qag, resolution 3.00Å" /> | ||
'''Actin binding region of the dystrophin homologue utrophin'''<br /> | '''Actin binding region of the dystrophin homologue utrophin'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Utrophin is a large multidomain protein that belongs to a | BACKGROUND: Utrophin is a large multidomain protein that belongs to a superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin. All the members of this family contain a common actin-binding region at their N termini and perform a wide variety of roles associated with the actin cytoskeleton. Utrophin is the autosomal homologue of dystrophin, the protein defective in the X-linked Duchenne and Becker muscular dystrophies, and upregulation of utrophin has been suggested as a potential therapy for muscular dystrophy patients. RESULTS: The structure of the actin-binding region of utrophin, consisting of two calponin-homology (CH) domains, has been solved at 3.0 A resolution. It is composed of an antiparallel dimer with each of the monomers being present in an extended dumbell shape and the two CH domains being separated by a long central helix. This extended conformation is in sharp contrast to the compact monomer structure of the N-terminal actin-binding region of fimbrin. CONCLUSIONS: The crystal structure of the actin-binding region of utrophin suggests that these actin-binding domains may be more flexible than was previously thought and that this flexibility may allow domain reorganisation and play a role in the actin-binding mechanism. Thus utrophin could possibly bind to actin in an extended conformation so that the sites previously identified as being important for actin binding may be directly involved in this interaction. | ||
==About this Structure== | ==About this Structure== | ||
1QAG 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:// | 1QAG 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=1QAG 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: Moores, C | [[Category: Moores, C A.]] | ||
[[Category: Norwood, F | [[Category: Norwood, F L.M.]] | ||
[[Category: Walke, S.]] | [[Category: Walke, S.]] | ||
[[Category: Winder, S | [[Category: Winder, S J.]] | ||
[[Category: actin binding]] | [[Category: actin binding]] | ||
[[Category: calponin homology domain]] | [[Category: calponin homology domain]] | ||
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[[Category: utrophin]] | [[Category: utrophin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:36 2008'' | ||
