PF00629

MAM domain, meprin/A5/mu

Pfam entry
Member databasePfam
Pfam typedomain
Short nameMAM
ClanConcanavalin
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description

An extracellular domain found in many receptors
[1]
. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerisation of the phosphatase ectoprotein and in cell adhesion
[4, 2]
. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases
[3]
.

References

1.An adhesive domain detected in functionally diverse receptors. Beckmann G, Bork P. Trends Biochem. Sci. 18, 40-1, (1993). View articlePMID: 8387703

2.Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion. Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY. EMBO J. 25, 701-12, (2006). View articlePMID: 16456543

3.Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane. Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stocker W, Becker-Pauly C, Gomis-Ruth FX. Proc. Natl. Acad. Sci. U.S.A. 109, 16131-6, (2012). View articlePMID: 22988105

4.Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism. Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY. Science 317, 1217-20, (2007). View articlePMID: 17761881

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