title: A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1.
abstract: 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.
authors.affiliation: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: rkahn@emory.edu.
authors.forename: Richard A
authors.initials: RA
authors.lastname: Kahn
authors.affiliation: Program in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: david.lambright@umassmed.edu.
authors.forename: David G
authors.initials: DG
authors.lastname: Lambright
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry*; D001665:Binding Sites; D008958:Models, Molecular; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D010743:Phospholipids