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1lcs
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(New page: 200px<br /><applet load="1lcs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcs, resolution 2.5Å" /> '''RECEPTOR-BINDING DOMA...)
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Revision as of 18:21, 20 November 2007
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RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS
Overview
Infection of T lymphocytes by the cytopathic retrovirus feline leukemia, virus subgroup T (FeLV-T) requires FeLIX, a cellular coreceptor that is, encoded by an endogenous provirus and closely resembles the, receptor-binding domain (RBD) of feline leukemia virus subgroup B, (FeLV-B). We determined the structure of FeLV-B RBD, which has FeLIX, activity, to a 2.5-A resolution by X-ray crystallography. The structure of, the receptor-specific subdomain of this glycoprotein differs dramatically, from that of Friend murine leukemia virus (Fr-MLV), which binds a, different cell surface receptor. Remarkably, we find that Fr-MLV RBD also, activates FeLV-T infection of cells expressing the Fr-MLV receptor and, that FeLV-B RBD is a competitive inhibitor of infection under these, conditions. These studies suggest that FeLV-T infection relies on the, following property of mammalian leukemia virus RBDs: the ability to couple, interaction with one of a variety of receptors to the activation of a, conserved membrane fusion mechanism. A comparison of the FeLV-B and Fr-MLV, RBD structures illustrates how receptor-specific regions are linked to, conserved elements critical for postbinding events in virus entry.
About this Structure
1LCS is a Single protein structure of sequence from Viruses with TOE as ligand. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of a coreceptor for infection by a pathogenic feline retrovirus., Barnett AL, Wensel DL, Li W, Fass D, Cunningham JM, J Virol. 2003 Feb;77(4):2717-29. PMID:12552012
Page seeded by OCA on Tue Nov 20 20:28:57 2007
