1hf0
From Proteopedia
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CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER
Overview
Two crystal structures of Oct-1 POU domain bound to DNA provide a, rationale for differential, conformation-dependent recruitment of, transcription cofactors. The POU-homeo and POU-specific subdomains of, Oct-1 contain two different nonoverlapping pairs of surface patches that, are capable of forming unrelated protein-protein interfaces. Members of, the POU factor family contain one or two conserved sequence motifs in the, interface that are known to be phosphorylated, as noted for Oct-1 and, Pit-1. Modeling of Oct-4 reveals the unique case where the same conserved, sequence is located in both interfaces. Our studies provide the basis for, two distinct dimeric POU factor arrangements that are dictated by the, architecture of each DNA response element. We suggest interface swapping, in dimers could be a general mechanism of modulating the activity of, transcription factors.
About this Structure
1HF0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping., Remenyi A, Tomilin A, Pohl E, Lins K, Philippsen A, Reinbold R, Scholer HR, Wilmanns M, Mol Cell. 2001 Sep;8(3):569-80. PMID:11583619
Page seeded by OCA on Mon Nov 12 17:17:15 2007
Categories: Homo sapiens | Single protein | Pohl, E. | Remenyi, A. | Scholer, H.R. | Tomilin, A. | Wilmanns, M. | Dimer | Oct-1 | Pou domain
