|EMBO Journal (2002) 21(18):4785-95|
|Northeast Structural Genomics Consortium|
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The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. ...
However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.
|metabolism chemistry genetics physiology |
|Binding Sites Crystallography, X-Ray Humans Protein Structure, Tertiary Amino Acid Sequence Animals Models, Molecular Molecular Sequence Data Nerve Tissue Proteins Protein Binding Protein Structure, Secondary Proteins Sequence Alignment Signal Transduction Intracellular Signaling Peptides and Proteins Membrane Proteins Carrier Proteins Mice Recombinant Fusion Proteins Chediak-Higashi Syndrome |
|63 (Last update: 03/16/2019 8:19:54pm)|
|EMBO J. 2002 Sep 16;21(18):4785-95.|