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1GH6

RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN

Summary for 1GH6
Entry DOI10.2210/pdb1gh6/pdb
DescriptorLarge T antigen, Retinoblastoma-associated protein (2 entities in total)
Functional Keywordstumor suppressor, oncoprotein, antitumor protein
Biological sourceSimian virus 40 (SV40)
More
Cellular locationHost nucleus : P03070
Nucleus : P06400
Total number of polymer chains2
Total formula weight52463.49
Authors
Kim, H.Y.,Cho, Y. (deposition date: 2000-11-15, release date: 2001-11-15, Last modification date: 2023-08-09)
Primary citationKim, H.Y.,Ahn, B.Y.,Cho, Y.
Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen.
EMBO J., 20:295-304, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11226179
DOI: 10.1093/emboj/20.1.295
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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