A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1

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Authors
Kahn, Richard A.
Lambright, David G.
UMass Chan Affiliations
Department of Biochemistry and Molecular Pharmacology
Program in Molecular Medicine
Document Type
Journal Article
Publication Date
2015-11-03
Keywords
Biochemistry
Molecular Biology
Structural Biology

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http://dx.doi.org/10.1016/j.str.2015.10.002
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.
Source
Structure. 2015 Nov 3;23(11):1971-3. doi: 10.1016/j.str.2015.10.002. Link to article on publisher's site
DOI
10.1016/j.str.2015.10.002
Permanent Link to this Item
http://hdl.handle.net/20.500.14038/44461
PubMed ID
26536378
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