pubmed-article:9461080 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1519025 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:9461080 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9461080 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9461080 | pubmed:dateCreated | 1998-2-20 | lld:pubmed |
pubmed-article:9461080 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9461080 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9461080 | pubmed:abstractText | The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process. | lld:pubmed |
pubmed-article:9461080 | pubmed:language | eng | lld:pubmed |
pubmed-article:9461080 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9461080 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9461080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9461080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9461080 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9461080 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9461080 | pubmed:issn | 1072-8368 | lld:pubmed |
pubmed-article:9461080 | pubmed:author | pubmed-author:WlodawerAA | lld:pubmed |
pubmed-article:9461080 | pubmed:author | pubmed-author:PlückthunAA | lld:pubmed |
pubmed-article:9461080 | pubmed:author | pubmed-author:HenneckeFF | lld:pubmed |
pubmed-article:9461080 | pubmed:author | pubmed-author:LubkowskiJJ | lld:pubmed |
pubmed-article:9461080 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9461080 | pubmed:volume | 5 | lld:pubmed |
pubmed-article:9461080 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9461080 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9461080 | pubmed:pagination | 140-7 | lld:pubmed |
pubmed-article:9461080 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:9461080 | pubmed:meshHeading | pubmed-meshheading:9461080-... | lld:pubmed |
pubmed-article:9461080 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9461080 | pubmed:articleTitle | The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. | lld:pubmed |
pubmed-article:9461080 | pubmed:affiliation | Macromolecular Structure Laboratory, ABL-Basic Research Program, NCI-FCRDC, Frederick, Maryland 21702, USA. | lld:pubmed |
pubmed-article:9461080 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9461080 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9461080 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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