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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Map (MHC class II analogous protein), also known as eap (extracellular adherence protein) and p70, is found in Staphylococcus aureus. It is a cell-wall associated protein, which is capable of binding to a number of different extracellular matrix glycoploteins and plasma proteins, and to the cell surface of S. aureus. Besides the broad binding specificity, map has been shown to be important in the adherence to and internalization of S. aureus by eukaryotic cells as well as being capable of modulating inflammatory response through its interactions with ICAM-1 (intercellular adhesion molecule-1), although its biological role in vivo remains to date unclear [ ].The protein consists of a signal peptide followed by a unique sequence of about 20 amino acids and four to six repeated MAP domains of 110-amino acid residues. Within each repeat there is a subdomain consisting of 31 residues that was found to be highly homologous to the N-terminal beta-chain of many MHC class II molecules [ ].This entry represents the MAP domain. The crystal structure of this domain has been solved and shows a core fold that is comprised of an α-helix lying diagonally across a five-stranded, mixed β-sheet. This structure is very similar to the C-terminal domain of bacterial superantigens [ ]. | Name | MAP domain |
| Short Name | MAP_dom | Type | Domain |
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