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. Author manuscript; available in PMC: 2010 Nov 1.
Published in final edited form as: Cell Signal. 2009 Jun 26;21(11):1569–1578. doi: 10.1016/j.cellsig.2009.06.003

Figure 1. An exposed hydrophobic patch on the PH domain is conserved within Lbc Family of RhoGEFs.

Figure 1

(A) Model of the LARG DH/PH domains in complex with RhoA at the cell membrane [28]. The side chains of Trp769 (yellow) in the hydrophobic core of the αN1/αN2 N-terminal extension, and Leu1086, Phe1098, Ile1100, and Ile1109 (red) in the hydrophobic patch of the PH domain are shown as ball-and-stick models. The latter residues form a hydrophobic patch oriented parallel to the predicted membrane surface (grey rectangle). The accessible surface of the DH/PH domains is shown semi-transparently. (B) A dimer interface mediated by the hydrophobic patch of the PH domain in the LARG DH/PH-RhoA crystals. The side chains of hydrophobic patch residues are shown as ball-and-stick models colored according to their subunit. In this interface, the β5, β6, and β7 strands of each PH domain are oriented in roughly parallel orientation. (C) Alignment of PH domain sequences spanning the hydrophobic patch residues from different members of the Lbc RhoGEF family. GenBank identifiers are as follows: LARG (34395525), PDZ-RhoGEF (34395516), p115-RhoGEF (34395524), GEF-H1 (6919894), Lbc-RhoGEF (6016482), p190-RhoGEF (172046113), and p114-RhoGEF (190358159). The positions of Leu1086, Phe1098, Ile1100, and Ile1109 are highlighted in red in the LARG sequence, and conserved residues in other Lbc family members are shown with bold text.