1aol

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Revision as of 11:53, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1aol" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aol, resolution 2.0Å" /> '''FRIEND MURINE LEUKEMI...)
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File:1aol.gif


1aol, resolution 2.0Å

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FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN

OverviewOverview

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 StructureAbout this Structure

1AOL is a Single protein structure of sequence from Friend murine leukemia virus with NAG and ZN as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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