Inhibitory complex of human meprin beta with mouse fetuin-B.

alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose

N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE

The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin beta by endogenous fetuin-B.

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases.

Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane.

Endopeptidase-2,Meprin B,N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta,PABA peptide hydrolase,PPH beta

20.0% PEG smear medium, 0.1M ammonium sulfate, 0.05M magnesium sulfate heptahydrate, 0.1M bicine pH 9.3, 10% ethylene glycol.

Heterotrameric assembly of dimeric meprin beta (protease) complexed at both active sites with fetuin-B (inhibitor).

protease inhibitor complex, zinc metallopeptidase, cystatin-type modules, HYDROLASE, HYDROLASE INHIBITOR