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  • Interacting selectively and non-covalently with a DH (Dbl homology) domain of a protein. The DH domain contains three structurally conserved regions separated by more variable regions. It is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH (pleckstrin homology) junction site, constitute the Rho GTPase interacting pocket. [GOC:yaf, InterPro:IPR000219, PMID:12775584]
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