1t77
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= LRBA, LBA, CDC4L, BGL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= LRBA, LBA, CDC4L, BGL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mi1|1MI1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t77 OCA], [http://www.ebi.ac.uk/pdbsum/1t77 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t77 RCSB]</span> | ||
}} | }} | ||
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[[Category: Shen, Y.]] | [[Category: Shen, Y.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| - | [[Category: ph-beach | + | [[Category: ph-beach domain]] |
| + | [[Category: signal transduction]] | ||
| + | [[Category: vesicle trafficking]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:52:17 2008'' |
Revision as of 20:52, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | LRBA, LBA, CDC4L, BGL (Homo sapiens) | ||||||
| Related: | 1MI1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:52:17 2008
