1x9p

From Proteopedia
Revision as of 06:47, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1x9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9p, resolution 3.30Å" /> '''The crystal structur...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1x9p.gif


1x9p, resolution 3.30Å

Drag the structure with the mouse to rotate

The crystal structure of human adenovirus 2 penton base

OverviewOverview

The adenovirus penton, a noncovalent complex of the pentameric penton base, and trimeric fiber proteins, comprises the vertices of the adenovirus, capsid and contains all necessary components for viral attachment and, internalization. The 3.3 A resolution crystal structure of human, adenovirus 2 (hAd2) penton base shows that the monomer has a basal, jellyroll domain and a distal irregular domain formed by two long, insertions, a similar topology to the adenovirus hexon. The Arg-Gly-Asp, (RGD) motif, required for interactions with cellular integrins, occurs on, a flexible surface loop. The complex of penton base with bound N-terminal, fiber peptide, determined at 3.5 A resolution, shows that the universal, fiber motif FNPVYPY binds at the interface of adjacent penton base, monomers and results in a localized structural rearrangement in the, insertion domain of the penton base. These results give insight into the, structure and assembly of the adenovirus capsid and will be of use for, gene-therapy applications.

About this StructureAbout this Structure

1X9P is a Single protein structure of sequence from Human adenovirus 2 with SO4 and C15 as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The structure of the human adenovirus 2 penton., Zubieta C, Schoehn G, Chroboczek J, Cusack S, Mol Cell. 2005 Jan 7;17(1):121-35. PMID:15629723

Page seeded by OCA on Wed Nov 21 05:55:13 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA