1mg1
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(New page: 200px<br /><applet load="1mg1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mg1, resolution 2.50Å" /> '''HTLV-1 GP21 ECTODOMA...)
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Revision as of 19:16, 20 November 2007
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HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA
Overview
Retroviral entry into cells depends on envelope glycoproteins, whereby, receptor binding to the surface-exposed subunit triggers membrane fusion, by the transmembrane protein (TM) subunit. We determined the crystal, structure at 2.5-A resolution of the ectodomain of gp21, the TM from human, T cell leukemia virus type 1. The gp21 fragment was crystallized as a, maltose-binding protein chimera, and the maltose-binding protein domain, was used to solve the initial phases by the method of molecular, replacement. The structure of gp21 comprises an N-terminal trimeric coiled, coil, an adjacent disulfide-bonded loop that stabilizes a chain reversal, and a C-terminal sequence structurally distinct from HIV type 1/simian, immunodeficiency virus gp41 that packs against the coil in an extended, antiparallel fashion. Comparison of the gp21 structure with the structures, of other retroviral TMs contrasts the conserved nature of the coiled, coil-forming region and adjacent disulfide-bonded loop with the variable, nature of the C-terminal ectodomain segment. The structure points to these, features having evolved to enable the dual roles of retroviral TMs:, conserved fusion function and an ability to anchor diverse surface-exposed, subunit structures to the virion envelope and infected cell surface. The, structure of gp21 implies that the N-terminal fusion peptide is in close, proximity to the C-terminal transmembrane domain and likely represents a, postfusion conformation.
About this Structure
1MG1 is a Single protein structure of sequence from Human t-lymphotropic virus 1 with MAL and CL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins., Kobe B, Center RJ, Kemp BE, Poumbourios P, Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4319-24. PMID:10200260
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