pubmed-article:12769718 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12769718 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:12769718 | lifeskim:mentions | umls-concept:C0332529 | lld:lifeskim |
pubmed-article:12769718 | lifeskim:mentions | umls-concept:C1704243 | lld:lifeskim |
pubmed-article:12769718 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12769718 | pubmed:dateCreated | 2003-5-28 | lld:pubmed |
pubmed-article:12769718 | pubmed:abstractText | It was predicted that the folding space for various protein sequences is restricted and a maximum of 1000 protein folds could be expected. Although, there were about 648 folds identified, general functional features of individual folds is not thoroughly studied. We selected OB-fold, which is supposed to be an oligonucleotide and oligosaccharide binding fold to study the general functional features. OB-fold is a small beta-barrel fold formed from 5 strands connected by modulating loops. We observed consistently 2 or 3 loops on the same face of barrel acting as clamps to bind to their ligands. Depending on the ligand, which could be a single or double stranded DNA/RNA or an oligosaccharide, and their conformational properties the loops change in length and sequence to accommodate various ligands. Different classes of OB-folded proteins were analyzed and found that the functional features are retained in spite of negligible sequence homology among various proteins studied. | lld:pubmed |
pubmed-article:12769718 | pubmed:language | eng | lld:pubmed |
pubmed-article:12769718 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12769718 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12769718 | pubmed:month | Jun | lld:pubmed |
pubmed-article:12769718 | pubmed:issn | 1389-2037 | lld:pubmed |
pubmed-article:12769718 | pubmed:author | pubmed-author:AgrawalVishal... | lld:pubmed |
pubmed-article:12769718 | pubmed:author | pubmed-author:KishanK V... | lld:pubmed |
pubmed-article:12769718 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12769718 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:12769718 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12769718 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12769718 | pubmed:pagination | 195-206 | lld:pubmed |
pubmed-article:12769718 | pubmed:dateRevised | 2005-11-16 | lld:pubmed |
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pubmed-article:12769718 | pubmed:meshHeading | pubmed-meshheading:12769718... | lld:pubmed |
pubmed-article:12769718 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12769718 | pubmed:articleTitle | OB-fold: growing bigger with functional consistency. | lld:pubmed |
pubmed-article:12769718 | pubmed:affiliation | Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India. | lld:pubmed |
pubmed-article:12769718 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12769718 | pubmed:publicationType | Review | lld:pubmed |
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