{PDOC51072}
{PS51072; MHD}
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* Mu homology domain (MHD) profile *
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The mu  homology  domain  (MHD) is an ~280 residue protein-protein interaction
module, which  is  found in endocytotic proteins involved in clathrin-mediated
endocytosis [1,2,3,4]:

 - Mu  subunits  of adaptor protein (AP) complexes, AP-1, AP-2, AP-3, and AP-4
   (see <PDOC00761>).
 - Proteins of the stonin family.
 - Proteins of the muniscin family: Syp1, FCHO1/2 and SGIP1.

The MHD  domain has an elongated, banana-shaped, all beta-sheet structure (see
<PDB:1BW8>). It  can  be considered as two beta-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
beta-sheet that  runs  the  whole  length  of the molecule. The tyrosine based
signal binds  to  a  site  on  the  surface of two parallel beta-sheet strands
(beta1 and beta16) in subdomain A [4,5].

The profile we developed covers the entire MHD domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2013 / Text revised.

[ 1] Martina J.A., Bonangelino C.J., Aguilar R.C., Bonifacino J.S.
     "Stonin 2: an adaptor-like protein that interacts with components of
     the endocytic machinery."
     J. Cell Biol. 153:1111-1120(2001).
     PubMed=11381094
[ 2] Walther K., Krauss M., Diril M.K., Lemke S., Ricotta D., Honing S.,
     Kaiser S., Haucke V.
     "Human stoned B interacts with AP-2 and synaptotagmin and facilitates
     clathrin-coated vesicle uncoating."
     EMBO Rep. 2:634-640(2001).
     PubMed=11454741; DOI=10.1093/embo-reports/kve134
[ 3] Walther K., Diril M.K., Jung N., Haucke V.
     "Functional dissection of the interactions of stonin 2 with the
     adaptor complex AP-2 and synaptotagmin."
     Proc. Natl. Acad. Sci. U.S.A. 101:964-969(2004).
     PubMed=14726597; DOI=10.1073/pnas.0307862100
[ 4] Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L.,
     Hurley J.H., Traub L.M., Wendland B.
     "Syp1 is a conserved endocytic adaptor that contains domains involved
     in cargo selection and membrane tubulation."
     EMBO J. 28:3103-3116(2009).
     PubMed=19713939; DOI=10.1038/emboj.2009.248
[ 5] Owen D.J., Evans P.R.
     "A structural explanation for the recognition of tyrosine-based
     endocytotic signals."
     Science 282:1327-1332(1998).
     PubMed=9812899

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