Structure and mutagenesis of the Dbl homology domain.
In: Nature Structural Biology, Jg. 5 (1998-12-01), Heft 12, S. 1098-1107
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Zugriff:
Guanine nucleotide exchange factors in the Dbl family activate Rho GTPases by accelerating dissociation of bound GDP, promoting acquisition of the GTP-bound state. Dbl proteins possess a ∼200 residue catalytic Dbl-homology (DH) domain, that is arranged in tandem with a C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we report the solution structure of the DH domain of human PAK-interacting exchange protein (βPIX). The domain is composed of 11 α-helices that form a flattened, elongated bundle. The structure explains a large body of mutagenesis data, which, along with sequence comparisons, identify the GTPase interaction site as a surface formed by three conserved helices near the center of one face of the domain. Proximity of the site to the DH C-terminus suggests a means by which PH-ligand interactions may be coupled to DH-GTPase interactions to regulate signaling through the Dbl proteins in vivo. [ABSTRACT FROM AUTHOR]
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Structure and mutagenesis of the Dbl homology domain.
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Autor/in / Beteiligte Person: | Aghazadeh, Behzad ; Zhu, Kejin ; Kubiseski, Terrance J. ; Liu, Grace A. ; Pawson, Tony ; Zheng, Yi ; Rosen, Michael K. |
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Zeitschrift: | Nature Structural Biology, Jg. 5 (1998-12-01), Heft 12, S. 1098-1107 |
Veröffentlichung: | 1998 |
Medientyp: | academicJournal |
ISSN: | 1072-8368 (print) |
DOI: | 10.1038/4209 |
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