1aol
From Proteopedia
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[[Image:1aol.gif|left|200px]] | [[Image:1aol.gif|left|200px]] | ||
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'''FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN''' | '''FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN''' | ||
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[[Category: Hamson, C A.]] | [[Category: Hamson, C A.]] | ||
[[Category: Kim, P S.]] | [[Category: Kim, P S.]] | ||
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| - | [[Category: | + | [[Category: Retrovirus]] |
| - | [[Category: | + | [[Category: Viral glycoprotein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:31:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:31, 2 May 2008
FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN
Overview
An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.
About this Structure
1AOL is a Single protein structure of sequence from Friend murine leukemia virus. Full crystallographic information is available from OCA.
Reference
Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution., Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM, Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219 Page seeded by OCA on Fri May 2 10:31:05 2008
