Purification, crystallization and preliminary X‐ray analysis of the inverse F‐BAR domain of the human srGAP2 protein. Issue 1 (1st January 2014)

• Record Type: Journal Article
• Authors: Wang, Hongpeng; Zhang, Yan; Zhang, Zhenyi; Jin, Wei‐Lin; Wu, Geng
• Is Part Of: Acta crystallographica. Volume 70:Issue 1(2014:Jan.)
• Page Start: 123
• Page End: 126
• Publication Date: 2014-01-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X13033712
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Bin–Amphiphysin–Rvs (BAR) domain proteins play essential roles in diverse cellular processes by inducing membrane invaginations or membrane protrusions. Among the BAR superfamily, the `classical' BAR and Fes/CIP4 homology BAR (F‐BAR) subfamilies of proteins usually promote membrane invaginations, whereas the inverse BAR (I‐BAR) subfamily generally incur membrane protrusions. Despite possessing an N‐terminal F‐BAR domain, the srGAP2 protein regulates neurite outgrowth and neuronal migration by causing membrane protrusions reminiscent of the activity of I‐BAR domain proteins. In this study, the inverse F‐BAR (IF‐BAR) domain of human srGAP2 was overexpressed, purified and crystallized. The crystals of the srGAP2 IF‐BAR domain protein diffracted to 3.50 Å resolution and belonged to space group <italic>P</italic>2₁. These results will facilitate further structural determination of the srGAP2 IF‐BAR domain and the ultimate elucidation of its peculiar behaviour of inducing membrane protrusions rather than membrane invaginations.</p> </abstract>