NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Related Articles NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Cell. 1998 Oct 16;95(2):269-77
Authors: Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW
Guanine nucleotide exchange factors for the Rho family of GTPases contain a Dbl homology (DH) domain responsible for catalysis and a pleckstrin homology (PH) domain whose function is unknown. Here we describe the solution structure of the N-terminal DH domain of Trio that catalyzes nucleotide exchange for Rac1. The all-alpha-helical protein has a very different structure compared to other exchange factors. Based on site-directed mutagenesis, functionally important residues of the DH domain were identified. They are all highly conserved and reside in close proximity on two a helices. In addition, we have discovered a unique capability of the PH domain to enhance nucleotide exchange in DH domain-containing proteins.
PMID: 9790533 [PubMed - indexed for MEDLINE]
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PubMed