| Literature DB >> 11350080 |
Abstract
This paper reports the identification of a Rho family nucleotide exchange factor termed mNET1 as a candidate-interacting partner for the first PDZ domain of MAGI-1, a membrane-associated guanylate kinase with inverted arrangement of protein-protein interacting modules. mNET1 was identified in a yeast two-hybrid screen and has a consensus tripeptide for PDZ domain binding at its extreme carboxy-terminus. In addition to this sequence, a cluster of basic residues located near the carboxy terminus is essential for the binding. The interaction of the first PDZ domain of MAGI-1with mNET1 was documented using a variety of biochemical methods. Copyright 2001 Academic Press.Entities:
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Year: 2001 PMID: 11350080 DOI: 10.1006/bbrc.2001.4880
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575