A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1
Kahn, Richard A. Lambright, David G.
Kahn, Richard A.
Lambright, David G.
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UMass Chan Affiliations
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Journal Article
Publication Date
2015-11-03
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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
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DOI
10.1016/j.str.2015.10.002
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PubMed ID
26536378