1HRZ
THE 3D STRUCTURE OF THE HUMAN SRY-DNA COMPLEX SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND-FILTERED NMR
Summary for 1HRZ
| Entry DOI | 10.2210/pdb1hrz/pdb |
| Descriptor | DNA (5'-D(*GP*CP*AP*CP*AP*AP*AP*C)-3'), DNA (5'-D(*GP*TP*TP*TP*GP*TP*GP*C)-3'), HUMAN SRY (3 entities in total) |
| Functional Keywords | dna binding protein/dna, dna binding protein-dna complex |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus speckle: Q05066 |
| Total number of polymer chains | 3 |
| Total formula weight | 14361.27 |
| Authors | Clore, G.M.,Werner, M.H.,Huth, J.R.,Gronenborn, A.M. (deposition date: 1995-05-09, release date: 1995-09-15, Last modification date: 2024-05-22) |
| Primary citation | Werner, M.H.,Huth, J.R.,Gronenborn, A.M.,Clore, G.M. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell(Cambridge,Mass.), 81:704-705, 1995 Cited by PubMed Abstract: 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 müllerian 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. PubMed: 7774012DOI: 10.1016/0092-8674(95)90532-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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