The mu homology domain (MHD) is an ~280 residue protein-protein interaction
module, which is found in endocytotic proteins involved in clathrin-mediated
Mu subunits of adaptor protein (AP) complexes, AP-1, AP-2, AP-3, and AP-4
Proteins of the stonin family.
Proteins of the muniscin family: Syp1, FCHO1/2 and SGIP1.
The MHD domain has an elongated, banana-shaped, all β-sheet structure (see
<PDB:1BW8>). It can be considered as two β-sandwich subdomains (A and B),
with subdomain B inserted between strands 6 and 15 of subdomain A, and joined
edge to edge such that the convex surface is a continuous nine-stranded mixed
β-sheet that runs the whole length of the molecule. The tyrosine based
signal binds to a site on the surface of two parallel β-sheet strands
(β1 and β16) in subdomain A [4,5].
The profile we developed covers the entire MHD domain.
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