| pubmed-article:15697204 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0065661 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15697204 | lifeskim:mentions | umls-concept:C0205144 | lld:lifeskim |
| pubmed-article:15697204 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15697204 | pubmed:dateCreated | 2005-2-8 | lld:pubmed |
| pubmed-article:15697204 | pubmed:abstractText | Missense mutations in the collagen triple-helix that replace one of the required Gly residues in the (Gly-Xaa-Yaa)(n)() repeating sequence have been implicated in various disorders. Although most hereditary collagen disorders are rare, a common occurrence of a Gly replacement mutation is found in the collagenous domain of mannose binding lectin (MBL). A Gly --> Asp mutation at position 54 in MBL is found at a frequency as high as 30% in certain populations and leads to increased susceptibility to infections. The structural and energetic consequences of this mutation are investigated by comparing a triple-helical peptide containing the N-terminal Gly-X-Y units of MBL with the homologous peptide containing the Gly to Asp replacement. The mutation leads to a loss of triple-helix content but only a small decrease in the stability of the triple-helix (DeltaT(m) approximately 2 degrees C) and no change in the calorimetric enthalpy. NMR studies on specifically labeled residues indicate the portion of the peptide C-terminal to residue 54 is in a highly ordered triple-helix in both peptides, while residues N-terminal to the mutation site have a weak triple-helical signal in the parent peptide and are completely disordered in the mutant peptide. These results suggest that the N-terminal triplet residues are contributing little to the stability of this peptide, a hypothesis confirmed by the stability and enthalpy of shorter peptides containing only the region C-terminal to the mutation site. The Gly to Asp replacement at position 54 in MBL occurs at the boundary of a highly stable triple-helix region and a very unstable sequence. The junctional position of this mutation minimizes its destabilizing effect, in contrast with the significant destabilization seen for Gly replacements in peptides modeling collagen diseases. | lld:pubmed |
| pubmed-article:15697204 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15697204 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15697204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15697204 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15697204 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15697204 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15697204 | pubmed:author | pubmed-author:AlfaroJ DJD | lld:pubmed |
| pubmed-article:15697204 | pubmed:author | pubmed-author:BrodskyBarbar... | lld:pubmed |
| pubmed-article:15697204 | pubmed:author | pubmed-author:BaumJeanJ | lld:pubmed |
| pubmed-article:15697204 | pubmed:author | pubmed-author:LiYingjieY | lld:pubmed |
| pubmed-article:15697204 | pubmed:author | pubmed-author:Doss-PepeElle... | lld:pubmed |
| pubmed-article:15697204 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15697204 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15697204 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:15697204 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15697204 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15697204 | pubmed:pagination | 1793-9 | lld:pubmed |
| pubmed-article:15697204 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:meshHeading | pubmed-meshheading:15697204... | lld:pubmed |
| pubmed-article:15697204 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15697204 | pubmed:articleTitle | Stability junction at a common mutation site in the collagenous domain of the mannose binding lectin. | lld:pubmed |
| pubmed-article:15697204 | pubmed:affiliation | Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA. | lld:pubmed |
| pubmed-article:15697204 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15697204 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15697204 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:4153 | entrezgene:pubmed | pubmed-article:15697204 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15697204 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15697204 | lld:pubmed |
