A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1
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UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyProgram in Molecular Medicine
Document Type
Journal ArticlePublication Date
2015-11-03
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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 siteDOI
10.1016/j.str.2015.10.002Permanent Link to this Item
http://hdl.handle.net/20.500.14038/44461PubMed ID
26536378Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.str.2015.10.002