| pubmed-article:12177432 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12177432 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:12177432 | lifeskim:mentions | umls-concept:C1511738 | lld:lifeskim |
| pubmed-article:12177432 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12177432 | lifeskim:mentions | umls-concept:C0205372 | lld:lifeskim |
| pubmed-article:12177432 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:12177432 | pubmed:dateCreated | 2002-8-21 | lld:pubmed |
| pubmed-article:12177432 | pubmed:abstractText | The death domain (DD) of the protein kinase Pelle adopts a six-helix bundle fold in the crystal structure of the complex with its dimerization partner, Tube-DD. However, in crystals obtained from a solution of 45% 2-methyl-2,4-pentanediol (MPD), the C-terminal half of Pelle-DD folds into a single helix, and the N-terminal half of the molecule is disordered. The helical segment forms an antiparallel dimer with the corresponding helix of a symmetry-related molecule, and together they form extensive lattice interactions similar in number, composition, and buried surface to those in the six-helix bundle of the native fold. Secondary structure analysis by heteronuclear nuclear magnetic resonance spectroscopy (NMR) demonstrates that Pelle-DD adopts a six-helix bundle fold in aqueous solution. The fold is perturbed by MPD, with the largest chemical shift changes in one helix and two loop regions that encompass the Tube-DD binding site. Pelle-DD is stable to urea denaturation with a folding free energy of 7.9 kcal/mol at 25 degrees C but is destabilized, with loss of urea binding sites, in the presence of MPD. The data are consistent with a cosolvent denaturation model in which MPD denatures the N terminus of Pelle-DD but induces the C terminus to form a more compact structure and aggregate. A similar perturbation in vivo might occur at the plasma membrane and could have consequences for Pelle-mediated regulation. Generally, crystallographers should be aware that high concentrations of MPD or related cosolvents can alter the tertiary structure of susceptible proteins. | lld:pubmed |
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| pubmed-article:12177432 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12177432 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12177432 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12177432 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12177432 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12177432 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12177432 | pubmed:author | pubmed-author:SprangStephen... | lld:pubmed |
| pubmed-article:12177432 | pubmed:author | pubmed-author:GardnerKevin... | lld:pubmed |
| pubmed-article:12177432 | pubmed:author | pubmed-author:XiaoTsanT | lld:pubmed |
| pubmed-article:12177432 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12177432 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:12177432 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12177432 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12177432 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12177432 | pubmed:pagination | 11151-6 | lld:pubmed |
| pubmed-article:12177432 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12177432 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12177432 | pubmed:articleTitle | Cosolvent-induced transformation of a death domain tertiary structure. | lld:pubmed |
| pubmed-article:12177432 | pubmed:affiliation | The Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA. | lld:pubmed |
| pubmed-article:12177432 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12177432 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:43283 | entrezgene:pubmed | pubmed-article:12177432 | lld:entrezgene |
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