1t77
From Proteopedia
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Crystal structure of the PH-BEACH domains of human LRBA/BGL
Overview
The beige and Chediak-Higashi syndrome (BEACH) domain defines a large, family of eukaryotic proteins that have diverse cellular functions in, vesicle trafficking, membrane dynamics, and receptor signaling. The domain, is the only module that is highly conserved among all of these proteins, but the exact functions of this domain and the molecular basis for its, actions are currently unknown. Our previous studies showed that the BEACH, domain is preceded by a novel, weakly conserved pleckstrin homology (PH), domain. We report here the crystal structure at 2.4 A resolution of the, PH-BEACH domain of human LRBA/BGL. The PH domain has the same backbone, fold as canonical PH domains, despite sharing no sequence homology with, them. However, our binding assays demonstrate that the PH domain in the, BEACH proteins cannot bind phospholipids. The BEACH domain contains a core, of several partially extended peptide segments that is flanked by helices, on both sides. The structure suggests intimate association between the PH, and the BEACH domains, and surface plasmon resonance studies confirm that, the two domains of the protein FAN have high affinity for each other, with, a K(d) of 120 nM.
About this Structure
1T77 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the PH-BEACH domains of human LRBA/BGL., Gebauer D, Li J, Jogl G, Shen Y, Myszka DG, Tong L, Biochemistry. 2004 Nov 30;43(47):14873-80. PMID:15554694
Page seeded by OCA on Mon Nov 12 19:21:31 2007
