1gh6
From Proteopedia
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| , resolution 3.2Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN
Overview
Inactivation of the retinoblastoma (Rb) tumor suppressor by Simian virus 40 (SV40) large T antigen is one of the central features of tumorigenesis induced by SV40. Both the N-terminal J domain and the LxCxE motif of large T antigen are required for inactivation of Rb. The crystal structure of the N-terminal region (residues 7-117) of SV40 large T antigen bound to the pocket domain of Rb reveals that large T antigen contains a four-helix bundle, and residues from helices alpha2 and alpha4 and from a loop containing the LxCxE motif participate in the interactions with Rb. The two central helices and a connecting loop in large T antigen have structural similarities with the J domains of the molecular chaperones DnaJ and HDJ-1, suggesting that large T antigen may use a chaperone mechanism for its biological function. However, there are significant differences between large T antigen and the molecular chaperones in other regions and these differences are likely to provide the specificity needed for large T antigen to inactivate Rb.
About this Structure
1GH6 is a Protein complex structure of sequences from Homo sapiens and Simian virus 40. The following page contains interesting information on the relation of 1GH6 with [Simian Virus 40]. Full crystallographic information is available from OCA.
Reference
Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen., Kim HY, Ahn BY, Cho Y, EMBO J. 2001 Jan 15;20(1-2):295-304. PMID:11226179
Page seeded by OCA on Sun Mar 30 20:43:51 2008
