1GH6
RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN
Summary for 1GH6
Entry DOI | 10.2210/pdb1gh6/pdb |
Descriptor | Large T antigen, Retinoblastoma-associated protein (2 entities in total) |
Functional Keywords | tumor suppressor, oncoprotein, antitumor protein |
Biological source | Simian virus 40 (SV40) More |
Cellular location | Host nucleus : P03070 Nucleus : P06400 |
Total number of polymer chains | 2 |
Total formula weight | 52463.49 |
Authors | |
Primary citation | Kim, 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: 11226179DOI: 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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