1afv

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spinqualitylabelsall models 1afv, resolution 3.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3

Overview

X-ray diffraction analysis of a human immunodeficiency virus (HIV-1), capsid (CA) protein shows that each monomer within the dimer consists of, seven alpha-helices, five of which are arranged in a coiled coil-like, structure. Sequence assignments were made for two of the helices, and, tentative connectivity of the remainder of the protein was confirmed by, the recent solution structure of a monomeric N-terminal fragment. The, C-terminal third of the protein is mostly disordered in the crystal. The, longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody, fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the, matrix protein and CA establish the side of the dimer that would be on the, exterior of the retroviral core.

About this Structure

1AFV is a Protein complex structure of sequences from Human immunodeficiency virus 1 and Mus musculus with PB as ligand. Structure known Active Sites: CP1 and CP2. Full crystallographic information is available from OCA.

Reference

Crystal structure of dimeric HIV-1 capsid protein., Momany C, Kovari LC, Prongay AJ, Keller W, Gitti RK, Lee BM, Gorbalenya AE, Tong L, McClure J, Ehrlich LS, Summers MF, Carter C, Rossmann MG, Nat Struct Biol. 1996 Sep;3(9):763-70. PMID:8784350

Page seeded by OCA on Mon Nov 5 15:17:26 2007