Extracellular matrix metalloproteinase inducer (EMMPRIN) structure and peptide design.
(A) The schematic structure of human EMMPRIN shows that EMMPRIN consists of an extracellular domain, a transmembrane domain, a cytoplasmic domain and a signal peptide (based on ). The two extracellular domains (EC) contain immunoglobulin-like (Ig-like) domains. The numbers represent the positions of amino acid residues, and amino acids in circles in the two EC domains represent sites of glycosylation. (B) Amino acid sequence in murine EMMPRIN EC1 domain compared to human, with one peptide (40-55) selected based on the sequence responsible for the matrix metalloproteinase (MMP) induction function of EMMPRIN, and the region that has the most homology between mouse and human EMMPRIN.