1r4r
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(New page: 200px<br /><applet load="1r4r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4r, resolution 3.0Å" /> '''Crystallographic anal...)
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Revision as of 23:08, 20 November 2007
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Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
Overview
Two crystal structures of the glucocorticoid receptor DNA-binding domain, complexed with DNA are reported. The domain has a globular fold which, contains two Zn-nucleated substructures of distinct conformation and, function. When it binds DNA, the domain dimerizes, placing the subunits in, adjacent major grooves. In one complex, the DNA has the symmetrical, consensus target sequence; in the second, the central spacing between the, target's half-sites is larger by one base pair. This results in one, subunit interacting specifically with the consensus target half-site and, the other nonspecifically with a noncognate element. The DNA-induced dimer, fixes the separation of the subunits' recognition surfaces so that the, spacing between the half-sites becomes a critical feature of the target, sequence's identity.
About this Structure
1R4R is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA., Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB, Nature. 1991 Aug 8;352(6335):497-505. PMID:1865905
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