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BEACH Domain
Class:Phospholipid binding

No Image The Beach domain adopts a unique and unusual structure, where large segments of the domain are either buried or help enclose the hydrophobic core, yet these segments are not β-strands since they are not fully extended. There are seven of these partially extended segments (ε1 to ε7). ε1, ε4 and ε7 contain regions that are completely buried in the core of the domain, and contain the residues that are most conserved among the Beach domains. The structure also contains 11 α-helices (αA to αK) that are arranged on the periphery of the structure, and enclose the core of the domain. Usually immediately preceding a Beach domain is a weakly conserved PH domain. Extensive molecular interactions exist between the two domains such that they form a single unit.

Structure Reference: Jogl, G. et al. (2002) EMBO J. 21(18), 4785-4795. "BEACH domain of human neurobeachin". PDB: 1MI1.

Domain binding and function:
The Beach domain was originally discovered as a conserved region within the protein responsible for the Chediak-Higashi syndrome (CHS). The name Beach comes from "beige and CHS" domain, where beige is the name of the CHS disease in mice. The Beach domain consists of approximately 300 amino acids and is found in proteins involved in vesicle trafficking, membrane dynamics and receptor signaling. Although the function of the Beach domain is not known, structural studies demonstrated that 100 residues or so prior to the domain consists of a weakly conserved, yet structurally identifiable PH domain, which interacts with the Beach domain to form a single unit. A large groove exists between the PH/Beach interface, which may serve as a ligand binding site. The Beach domain is usually followed by a series of WD repeats.
Examples of Proteins:
CHS protein

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