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10.1074/jbc.M113.462002 http://scihub22266oqcxt.onion/10.1074/jbc.M113.462002 C3696688!3696688 !23645670     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23645670 &cmd=llinks): Failed to open stream: HTTP request failed! 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Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding |pdf=|usr=}}{{23645670 }} gab.com Text Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23645670 #FOAvip Vascular Ehlers-Danlos syndrome (EDS) type IV is the most severe form of EDS. In many cases the disease is caused by a point mutation of Gly in type III collagen. A slower folding of the collagen helix is a potential cause for over-modifications. However, little is known about the rate of folding of type III collagen in patients with EDS. To understand the molecular mechanism of the effect of mutations, a system was developed for bacterial production of homotrimeric model polypeptides. The C-terminal quarter, 252 residues, of the natural human type III collagen was attached to (GPP)7 with the type XIX collagen trimerization domain (NC2). The natural collagen domain forms a triple helical structure without 4-hydroxylation of proline at a low temperature. At 33 °C, the natural collagenous part is denatured, but the C-terminal (GPP)7-NC2 remains intact. Switching to a low temperature triggers the folding of the type III collagen domain in a zipper-like fashion that resembles the natural process. We used this system for the two known EDS mutations (Gly-to-Val) in the middle at Gly-910 and at the C terminus at Gly-1018. In addition, wild-type and Gly-to-Ala mutants were made. The mutations significantly slow down the overall rate of triple helix formation. The effect of the Gly-to-Val mutation is much more severe compared with Gly-to-Ala. This is the first report on the folding of collagen with EDS mutations, which demonstrates local delays in the triple helix propagation around the mutated residue. Twit Text FOAVip Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=23645670 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23645670 #FOAvip English Wikipedia <ref>{{Cite pmid|23645670 }}</ref> Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding #MMPMID23645670 Mizuno K ; Boudko S ; Engel J ; Bächinger HP J Biol Chem 2013[Jun]; 288 (26 ): 19166-76 PMID23645670 show ga Vascular Ehlers-Danlos syndrome (EDS) type IV is the most severe form of EDS. In many cases the disease is caused by a point mutation of Gly in type III collagen. A slower folding of the collagen helix is a potential cause for over-modifications. However, little is known about the rate of folding of type III collagen in patients with EDS. To understand the molecular mechanism of the effect of mutations, a system was developed for bacterial production of homotrimeric model polypeptides. The C-terminal quarter, 252 residues, of the natural human type III collagen was attached to (GPP)7 with the type XIX collagen trimerization domain (NC2). The natural collagen domain forms a triple helical structure without 4-hydroxylation of proline at a low temperature. At 33 °C, the natural collagenous part is denatured, but the C-terminal (GPP)7-NC2 remains intact. Switching to a low temperature triggers the folding of the type III collagen domain in a zipper-like fashion that resembles the natural process. We used this system for the two known EDS mutations (Gly-to-Val) in the middle at Gly-910 and at the C terminus at Gly-1018. In addition, wild-type and Gly-to-Ala mutants were made. The mutations significantly slow down the overall rate of triple helix formation. The effect of the Gly-to-Val mutation is much more severe compared with Gly-to-Ala. This is the first report on the folding of collagen with EDS mutations, which demonstrates local delays in the triple helix propagation around the mutated residue. |*Protein Folding [MESH] |Circular Dichroism [MESH] |Collagen Type III/chemistry/*genetics [MESH] |Collagen/chemistry [MESH] |Ehlers-Danlos Syndrome/*genetics [MESH] |Humans [MESH] |Mutation [MESH] |Peptidylprolyl Isomerase/chemistry [MESH] |Point Mutation [MESH] |Protein Processing, Post-Translational [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Recombinant Proteins/chemistry [MESH] |Temperature [MESH]Vascular Ehlers-Danlos syndrome mutations in type III collagen differe(epmc).pdf DeepDyve Pubget Overpricing