1mof
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(New page: 200px<br /><applet load="1mof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mof, resolution 1.7Å" /> '''COAT PROTEIN'''<br />...)
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Revision as of 19:27, 20 November 2007
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COAT PROTEIN
Overview
We report the crystal structure of an extraviral segment of a retrovirus, envelope protein, the Moloney murine leukemia virus (MoMuLV) transmembrane, (TM) subunit. This segment, which comprises a region of the MoMuLV TM, protein analogous to that contained within the X-ray crystal structure of, low-pH converted influenza hemagglutinin, contains a trimeric coiled coil, with a hydrophobic cluster at its base and a strand that packs in an, antiparallel orientation against the coiled coil. This structure gives the, first high-resolution insight into the retrovirus surface and serves as a, model for a wide range of viral fusion proteins; key residues in this, structure are conserved among C- and D-type retroviruses and the filovirus, ebola.
About this Structure
1MOF is a Single protein structure of sequence from Moloney murine leukemia virus with CL as ligand. Full crystallographic information is available from OCA.
Reference
Retrovirus envelope domain at 1.7 angstrom resolution., Fass D, Harrison SC, Kim PS, Nat Struct Biol. 1996 May;3(5):465-9. PMID:8612078
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