| pubmed-article:3863103 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3863103 | lifeskim:mentions | umls-concept:C0035542 | lld:lifeskim |
| pubmed-article:3863103 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:3863103 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3863103 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:3863103 | pubmed:dateCreated | 1985-10-31 | lld:pubmed |
| pubmed-article:3863103 | pubmed:abstractText | X-ray diffraction methods were used to test a synthetic-modeling approach to the sequence engineering of bovine pancreatic ribonuclease. A model of RNase S-peptide (residues 1-20), having a simplified amino acid sequence but retaining elements deduced to be essential for conformation and function, was previously synthesized and found to form a catalytically active and stable complex with native S-protein (residues 21-24). We have now obtained a 3-A-resolution electron density map of this semisynthetic complex which reveals that the conformation of model peptide closely mimics that of native S-peptide, as intended by sequence design. Some small differences from the native structure are observed: Glu-2 and Arg-10 of the model complex are not close enough to form a salt bridge, the position of the His-12 imidazole ring is slightly shifted in the active site, and the peptide's amino terminus is reoriented. Nonetheless, the major structural features predicted to be essential by computer-aided peptide-design analysis are preserved in the model peptide portion of the complex. These include (i) the alpha-helical framework involving residues 3-13, (ii) the catalytically competent orientation of His-12, and (iii) complex-stabilizing non-bonding interactions involving Phe-8 and Met-13 of S-peptide and hydrophobic residues in the cleft region of S-protein. Further, sequence simplification has not introduced any non-native, potentially stabilizing contacts between the model peptide and S-protein. The results emphasize the usefulness, in redesigning native proteins, of categorizing sequence into residues providing conformational framework and those determining intra-and intermolecular surface recognition. | lld:pubmed |
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| pubmed-article:3863103 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3863103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3863103 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3863103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3863103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3863103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3863103 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3863103 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:3863103 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3863103 | pubmed:author | pubmed-author:ChaikenI MIM | lld:pubmed |
| pubmed-article:3863103 | pubmed:author | pubmed-author:TaylorH CHC | lld:pubmed |
| pubmed-article:3863103 | pubmed:author | pubmed-author:KomoriyaAA | lld:pubmed |
| pubmed-article:3863103 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3863103 | pubmed:volume | 82 | lld:pubmed |
| pubmed-article:3863103 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3863103 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3863103 | pubmed:pagination | 6423-6 | lld:pubmed |
| pubmed-article:3863103 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:meshHeading | pubmed-meshheading:3863103-... | lld:pubmed |
| pubmed-article:3863103 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3863103 | pubmed:articleTitle | Crystallographic structure of an active, sequence-engineered ribonuclease. | lld:pubmed |
| pubmed-article:3863103 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3863103 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3863103 | lld:pubmed |
