1mg1
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1mg1.jpg|left|200px]] | + | [[Image:1mg1.jpg|left|200px]] |
| - | + | ||
| - | '''HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA''' | + | {{Structure |
| + | |PDB= 1mg1 |SIZE=350|CAPTION= <scene name='initialview01'>1mg1</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MG1 is a [ | + | 1MG1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_t-lymphotropic_virus_1 Human t-lymphotropic virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MG1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10200260 10200260] |
[[Category: Human t-lymphotropic virus 1]] | [[Category: Human t-lymphotropic virus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: membrane fusion]] | [[Category: membrane fusion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:43:06 2008'' |
Revision as of 10:43, 20 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:43:06 2008
