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1cit
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(New page: 200px<br /><applet load="1cit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cit, resolution 2.7Å" /> '''DNA-BINDING MECHANISM...)
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Revision as of 10:22, 20 November 2007
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DNA-BINDING MECHANISM OF THE MONOMERIC ORPHAN NUCLEAR RECEPTOR NGFI-B
Overview
The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the, orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed, to its high-affinity DNA target, represents the first structure analysis, of a nuclear receptor DBD bound as a monomer to DNA. The structure of the, core DBD and its interactions with the major groove of the DNA are similar, to previously crystallographically solved DBD-DNA complexes in this, superfamily; however, residues C-terminal to this core form a separate and, unique substructure that interacts extensively and in a sequence-specific, way with the minor groove of its DNA target, in particular with the, characteristic 3 A-T base-pair identity element that extends 5' to the, usual nuclear receptor half-site (AGGTCA).
About this Structure
1CIT is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B., Meinke G, Sigler PB, Nat Struct Biol. 1999 May;6(5):471-7. PMID:10331876
Page seeded by OCA on Tue Nov 20 12:29:54 2007
