3.4.24.63	?	x * 73000, SDS-PAGE	683206	
3.4.24.63	dimer	a model of the meprin B dimer structure is proposed that provides insight into the relationship between structure and function of thus isoforms	669315	
3.4.24.63	dimer	meprin beta is a multidomain metalloprotease and a dimeric type 1 transmembrane protein, enzyme domain structure, overview. The enzyme consists of a propeptide (PRO), a catalytic domain (CAT), a MAM (meprin A5 protein tyrosine phosphatase mu) domain, a TRAF (tumor-necrosis-factor-receptor-associated factor) domain, an EGF (epidermal growth factor) like domain, a transmembrane region and a C-terminal part	734610	
3.4.24.63	dimer	the mature protease forms dimers which are stabilized by an intermolecular disulfide bond between the MAM domains	754592	
3.4.24.63	homodimer	-	754236	
3.4.24.63	homodimer	domain composition and dimeric structure of the metalloprotease meprin beta, overview. The enzyme consists of propeptide, catalytic domain, meprin A5 protein tyrosine phosphatase micro domain, tumour-necrosis-factor-receptor-associated factor domain, epidermal growth factor-like domain, transmembrane region, and C-terminal part	753218	
3.4.24.63	homodimer	homodimer linked by a disulfide bridge, domain structure of human meprins, overview	733288	
3.4.24.63	homodimer	meprin beta is a homodimeric multidomain type-I membrane metallopeptidase	735161	
3.4.24.63	homodimer	the enzyme consists of the protease domain with a 39 amino acid long inhibitory pro-peptide, a MAM domain, a TRAF domain, an EGF-like domain, a transmembrane helix, and a small C-terminal cytosolic domain	753172	
3.4.24.63	additional information	all three meprin subunits identified in zebrafish contain the typical astacin domain, the Met-turn SxMHY, and the four cysteine residues that form two disulfide bonds	683206