| pubmed-article:1868826 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0699919 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:1868826 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:1868826 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:1868826 | pubmed:dateCreated | 1991-9-18 | lld:pubmed |
| pubmed-article:1868826 | pubmed:abstractText | From the lysosomal cysteine proteinase cathepsin B, isolated from human liver in its two-chain form, monoclinic crystals were obtained which contain two molecules per asymmetric unit. The molecular structure was solved by a combination of Patterson search and heavy atom replacement methods (simultaneously with rat cathepsin B) and refined to a crystallographic R value of 0.164 using X-ray data to 2.15 A resolution. The overall folding pattern of cathepsin B and the arrangement of the active site residues are similar to the related cysteine proteinases papain, actinidin and calotropin DI. 166 alpha-carbon atoms out of 248 defined cathepsin B residues are topologically equivalent (with an r.m.s. deviation of 1.04 A) with alpha-carbon atoms of papain. However, several large insertion loops are accommodated on the molecular surface and modify its properties. The disulphide connectivities recently determined for bovine cathepsin B by chemical means were shown to be correct. Some of the primed subsites are occluded by a novel insertion loop, which seems to favour binding of peptide substrates with two residues carboxy-terminal to the scissile peptide bond; two histidine residues (His110 and His111) in this "occluding loop' provide positively charged anchors for the C-terminal carboxylate group of such polypeptide substrates. These structural features explain the well-known dipeptidyl carboxypeptidase activity of cathepsin B. The other subsites adjacent to the reactive site Cys29 are relatively similar to papain; Glu245 in the S2 subsite favours basic P2-side chains. The above mentioned histidine residues, but also the buried Glu171 might represent the group with a pKa of approximately 5.5 near the active site, which governs endo- and exopeptidase activity. The "occluding loop' does not allow cystatin-like protein inhibitors to bind to cathepsin B as they do to papain, consistent with the reduced affinity of these protein inhibitors for cathepsin B compared with the related plant enzymes. | lld:pubmed |
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| pubmed-article:1868826 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1868826 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1868826 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1868826 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1868826 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1868826 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1868826 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:KatunumaNN | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:HuberRR | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:TowatariTT | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:TurkVV | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:MayrII | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:TurkDD | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:PopovicTT | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:EnghR ARA | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:MusilDD | lld:pubmed |
| pubmed-article:1868826 | pubmed:author | pubmed-author:ZucicDD | lld:pubmed |
| pubmed-article:1868826 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1868826 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:1868826 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1868826 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:1868826 | pubmed:pagination | 2321-30 | lld:pubmed |
| pubmed-article:1868826 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
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| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
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| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
| pubmed-article:1868826 | pubmed:meshHeading | pubmed-meshheading:1868826-... | lld:pubmed |
| pubmed-article:1868826 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1868826 | pubmed:articleTitle | The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. | lld:pubmed |
| pubmed-article:1868826 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Martinsried, FRG. | lld:pubmed |
| pubmed-article:1868826 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1868826 | pubmed:publicationType | Comparative Study | lld:pubmed |
