|PROSITE documentation PDOC50197|
The BEACH (for BEIge And CHS) domain is a region of about 300 residues that is highly conserved in a large family of eukaryotic proteins. Many of the proteins that contain a BEACH domain are very large (with >2000 residues) and have putative functions in vesicular transport, membrane dynamics and receptor signaling. The BEACH domain is crucial for the normal function of these proteins. In all known BEACH-containing proteins, the BEACH domain is located just prior to a WD-40 domain (see <PDOC00574>) in the primary sequence, which is located at the extreme C-terminus of most of these proteins. In addition, structural analysis revealed that BEACH domain has intimate contacts with a fold identical to that of PH domains (see <PDOC50003>) just prior to it in the primary sequence. 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. The function of the BEACH domain is unknown [1,2,3].
The resolution of the crystal structure of the BEACH domain of human Nbea (see <PDB:1MI1>) as shown that it has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures (α-helix or β-sheet). In addition, only a few main-chain hydrogen-bonds are made among these segments. The structure of the BEACH domain also contains 11 α-helices that are arranged on the periphery of the structure, but help to enclose the core of the domain .
Proteins known to contain a BEACH domain are listed below:
October 2002 / Profile and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Nagle D.L. Karim M.A. Woolf E.A. Holmgren L. Bork P. Misumi D.J. McGrail S.H. Dussault B.J. Jr. Perou C.M. Boissy R.E. Duyk G.M. Spritz R.A. Moore K.J.|
|Title||Identification and mutation analysis of the complete gene for Chediak-Higashi syndrome.|
|Source||Nat. Genet. 14:307-311(1996).|
|2||Authors||Adam-Klages S. Schwandner R. Adam D. Kreder D. Bernardo K. Kronke M.|
|Title||Distinct adapter proteins mediate acid versus neutral sphingomyelinase activation through the p55 receptor for tumor necrosis factor.|
|Source||J. Leukoc. Biol. 63:678-682(1998).|
|3||Authors||Jogl G. Shen Y. Gebauer D. Li J. Wiegmann K. Kashkar H. Kronke M. Tong L.|
|Title||Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.|
|Source||EMBO J. 21:4785-4795(2002).|