1hry
From Proteopedia
THE 3D STRUCTURE OF THE HUMAN SRY-DNA COMPLEX SOLVED BY MULTID-DIMENSIONAL HETERONUCLEAR-EDITED AND-FILTERED NMR
Overview
The solution structure of the specific complex between the high mobility group (HMG) domain of SRY (hSRY-HMG), the protein encoded by the human testis-determining gene, and its DNA target site in the promoter of the mullerian inhibitory substance gene has been determined by multidimensional NMR spectroscopy. hSRY-HMG has a twisted L shape that presents a concave surface (made up of three helices and the N- and C-terminal strands) to the DNA for sequence-specific recognition. Binding of hSRY-HMG to its specific target site occurs exclusively in the minor groove and induces a large conformational change in the DNA. The DNA in the complex has an overall 70 degrees-80 degrees bend and is helically unwound relative to classical A- and B-DNA. The structure of the complex reveals the origin of sequence-specific binding within the HMG-1/HMG-2 family and provides a framework for understanding the effects of point mutations that cause 46X,Y sex reversal at the atomic level.
About this Structure
1HRY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex., Werner MH, Huth JR, Gronenborn AM, Clore GM, Cell. 1995 Jun 2;81(5):705-14. PMID:7774012 Page seeded by OCA on Fri May 2 19:10:31 2008
Categories: Homo sapiens | Single protein | Clore, G M. | Gronenborn, A M. | Huth, J R. | Werner, M H. | Dna | Dna-binding protein | Nmr | Sry
