A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1
Program in Molecular Medicine; Department of Biochemistry and Molecular Pharmacology
Biochemistry | Molecular Biology | Structural Biology
In this issue of Structure, Jian et al. (2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1. This PH domain has two anionic phospholipid binding sites proposed to work in concert to regulate ASAP1 GAP activity.
DOI of Published Version
Structure. 2015 Nov 3;23(11):1971-3. doi: 10.1016/j.str.2015.10.002. Link to article on publisher's site
Structure (London, England : 1993)
Kahn, Richard A. and Lambright, David G., "A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1" (2015). Program in Molecular Medicine Publications and Presentations. 55.