| pubmed-article:8393577 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0007427 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0013171 | lld:lifeskim |
| pubmed-article:8393577 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:8393577 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:8393577 | pubmed:dateCreated | 1993-8-30 | lld:pubmed |
| pubmed-article:8393577 | pubmed:abstractText | Cathepsin D (EC 3.4.23.5) is a lysosomal protease suspected to play important roles in protein catabolism, antigen processing, degenerative diseases, and breast cancer progression. Determination of the crystal structures of cathepsin D and a complex with pepstatin at 2.5 A resolution provides insights into inhibitor binding and lysosomal targeting for this two-chain, N-glycosylated aspartic protease. Comparison with the structures of a complex of pepstatin bound to rhizopuspepsin and with a human renin-inhibitor complex revealed differences in subsite structures and inhibitor-enzyme interactions that are consistent with affinity differences and structure-activity relationships and suggest strategies for fine-tuning the specificity of cathepsin D inhibitors. Mutagenesis studies have identified a phosphotransferase recognition region that is required for oligosaccharide phosphorylation but is 32 A distant from the N-domain glycosylation site at Asn-70. Electron density for the crystal structure of cathepsin D indicated the presence of an N-linked oligosaccharide that extends from Asn-70 toward Lys-203, which is a key component of the phosphotransferase recognition region, and thus provides a structural explanation for how the phosphotransferase can recognize apparently distant sites on the protein surface. | lld:pubmed |
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| pubmed-article:8393577 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8393577 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8393577 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8393577 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8393577 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:CollinsJJ | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:EricksonJ WJW | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:BhatT NTN | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:HosurM VMV | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:SilvaA MAM | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:CachauR ERE | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:SowderR... | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:BaldwinE TET | lld:pubmed |
| pubmed-article:8393577 | pubmed:author | pubmed-author:GulnikSS | lld:pubmed |
| pubmed-article:8393577 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8393577 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8393577 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:8393577 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8393577 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8393577 | pubmed:pagination | 6796-800 | lld:pubmed |
| pubmed-article:8393577 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8393577 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8393577 | pubmed:articleTitle | Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design. | lld:pubmed |
| pubmed-article:8393577 | pubmed:affiliation | Structural Biochemistry Program, Program Resources Inc./DynCorp, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702. | lld:pubmed |
| pubmed-article:8393577 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8393577 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8393577 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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