1T77
Crystal structure of the PH-BEACH domains of human LRBA/BGL
Summary for 1T77
| Entry DOI | 10.2210/pdb1t77/pdb |
| Related | 1MI1 |
| Descriptor | Lipopolysaccharide-responsive and beige-like anchor protein (2 entities in total) |
| Functional Keywords | ph-beach domains; vesicle trafficking; signal transduction, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass membrane protein (Potential): P50851 |
| Total number of polymer chains | 4 |
| Total formula weight | 190855.17 |
| Authors | Gebauer, D.,Li, J.,Jogl, G.,Shen, Y.,Myszka, D.G.,Tong, L. (deposition date: 2004-05-08, release date: 2004-12-21, Last modification date: 2024-02-14) |
| Primary citation | Gebauer, D.,Li, J.,Jogl, G.,Shen, Y.,Myszka, D.G.,Tong, L. Crystal Structure of the PH-BEACH Domains of Human LRBA/BGL Biochemistry, 43:14873-14880, 2004 Cited by PubMed Abstract: 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. PubMed: 15554694DOI: 10.1021/bi049498y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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