Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate.

Journal article

Rab GTPases are key regulators of membrane traffic pathways within eukaryotic cells. They are specifically activated by guanine nucleotide exchange factors (GEFs), which convert them from their "inactive" GDP-bound form to the "active" GTP-bound form. In higher eukaryotes, proteins containing DENN-domains comprise a major GEF family. Here we describe at 2.1-Å resolution the first structure of a DENN-domain protein, DENND1B-S, complexed with its substrate Rab35, providing novel insights as to ...

Expand abstract

Authors: Wu, X; Bradley, M; Cai, Y; Kümmel, D; De La Cruz, E

• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 108
• Issue: 46
• Pages: 18672-18677
• Publication date: 2011-11-01
• DOI: 10.1073/pnas.1110415108
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Protein Binding; Death Domain Receptor Signaling Adaptor Proteins; Binding Sites; Protein Structure, Tertiary; Kinetics; Guanine; Crystallography, X-Ray; Humans; rab GTP-Binding Proteins; Guanine Nucleotide Exchange Factors; Protein Structure, Secondary; rab1 GTP-Binding Proteins; Nucleotides; Biological Transport