| pubmed-article:12391332 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C0600479 | lld:lifeskim |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C0562558 | lld:lifeskim |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:12391332 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:12391332 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:12391332 | pubmed:dateCreated | 2002-10-30 | lld:pubmed |
| pubmed-article:12391332 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:abstractText | Carbohydrate-protein recognition is central to many biological processes. Enzymes that act on polysaccharide substrates frequently contain noncatalytic domains, "carbohydrate-binding modules" (CBMs), that target the enzyme to the appropriate substrate. CBMs that recognize specific plant structural polysaccharides are often able to accommodate both the variable backbone and the side-chain decorations of heterogeneous ligands. "CBM29" modules, derived from a noncatalytic component of the Piromyces equi cellulase/hemicellulase complex, provide an example of this selective yet flexible recognition. They discriminate strongly against some polysaccharides while remaining relatively promiscuous toward both beta-1,4-linked manno- and cello-oligosaccharides. This feature may reflect preferential, but flexible, targeting toward glucomannans in the plant cell wall. The three-dimensional structure of CBM29-2 and its complexes with cello- and mannohexaose reveal a beta-jelly-roll topology, with an extended binding groove on the concave surface. The orientation of the aromatic residues complements the conformation of the target sugar polymer while accommodation of both manno- and gluco-configured oligo- and polysaccharides is conferred by virtue of the plasticity of the direct interactions from their axial and equatorial 2-hydroxyls, respectively. Such flexible ligand recognition targets the anaerobic fungal complex to a range of different components in the plant cell wall and thus plays a pivotal role in the highly efficient degradation of this composite structure by the microbial eukaryote. | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12391332 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12391332 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12391332 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12391332 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:CharnockSimon... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:DaviesGideon... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:NurizzoDidier... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:GilbertHarry... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:BolamDavid... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:McKieVincent... | lld:pubmed |
| pubmed-article:12391332 | pubmed:author | pubmed-author:SzabóLórándL | lld:pubmed |
| pubmed-article:12391332 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12391332 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:12391332 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12391332 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12391332 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12391332 | pubmed:pagination | 14077-82 | lld:pubmed |
| pubmed-article:12391332 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:meshHeading | pubmed-meshheading:12391332... | lld:pubmed |
| pubmed-article:12391332 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12391332 | pubmed:articleTitle | Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose. | lld:pubmed |
| pubmed-article:12391332 | pubmed:affiliation | Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, United Kingdom. | lld:pubmed |
| pubmed-article:12391332 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12391332 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12391332 | lld:pubmed |
