pubmed-article:3676333 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3676333 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
pubmed-article:3676333 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
pubmed-article:3676333 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:3676333 | lifeskim:mentions | umls-concept:C0205372 | lld:lifeskim |
pubmed-article:3676333 | lifeskim:mentions | umls-concept:C1517050 | lld:lifeskim |
pubmed-article:3676333 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3676333 | pubmed:dateCreated | 1987-12-30 | lld:pubmed |
pubmed-article:3676333 | pubmed:abstractText | Alignment of the sequences, the identification of conserved residue patterns and secondary structure predictions indicate that the extra-cellular regions of the human and Drosophila epidermal growth factor (EGF), c-erb-B2 and human insulin receptors each contain two large, homologous domains (L) which are probably comprised of at least four short alpha-helices followed by turns of conserved length and beta-strands. In the human and Drosophila EGF and c-erb-B2 receptors these homologous domains are each followed by a series of smaller cystine-rich domains (S) to give a gene-duplicated structure of L1S11S12S13L2S21S22S23. In the human insulin receptor, the second series of cystine domains is replaced by a different sequence. These duplicated structures are probably organised as a pseudo-symmetrical dimer. There are two 'hyper-variable' regions, one at the end of the large domains and one in the cystine-rich sequences, which are candidates for hormone or growth-factor binding. | lld:pubmed |
pubmed-article:3676333 | pubmed:language | eng | lld:pubmed |
pubmed-article:3676333 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3676333 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3676333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3676333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3676333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3676333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3676333 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3676333 | pubmed:month | Nov | lld:pubmed |
pubmed-article:3676333 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:3676333 | pubmed:author | pubmed-author:SchlessingerJ... | lld:pubmed |
pubmed-article:3676333 | pubmed:author | pubmed-author:WaterfieldM... | lld:pubmed |
pubmed-article:3676333 | pubmed:author | pubmed-author:BlundellTT | lld:pubmed |
pubmed-article:3676333 | pubmed:author | pubmed-author:BajanAA | lld:pubmed |
pubmed-article:3676333 | pubmed:author | pubmed-author:TaylorW RWR | lld:pubmed |
pubmed-article:3676333 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3676333 | pubmed:day | 26 | lld:pubmed |
pubmed-article:3676333 | pubmed:volume | 916 | lld:pubmed |
pubmed-article:3676333 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3676333 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3676333 | pubmed:pagination | 220-6 | lld:pubmed |
pubmed-article:3676333 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:3676333 | pubmed:meshHeading | pubmed-meshheading:3676333-... | lld:pubmed |
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pubmed-article:3676333 | pubmed:meshHeading | pubmed-meshheading:3676333-... | lld:pubmed |
pubmed-article:3676333 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3676333 | pubmed:articleTitle | On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. | lld:pubmed |
pubmed-article:3676333 | pubmed:affiliation | Ludwig Institute for Cancer Research, University College, London, U.K. | lld:pubmed |
pubmed-article:3676333 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3676333 | pubmed:publicationType | Comparative Study | lld:pubmed |
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