1afv

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Revision as of 22:35, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1afv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1afv, resolution 3.7Å" /> '''HIV-1 CAPSID PROTEIN...)
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File:1afv.gif


1afv, resolution 3.7Å

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

OverviewOverview

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, ... [(full description)]

About this StructureAbout this Structure

1AFV is a [Protein complex] structure of sequences from [Human immunodeficiency virus 1] and [Mus musculus] with PB as [ligand]. Full crystallographic information is available from [OCA].

ReferenceReference

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

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