2012
DOI: 10.1016/j.jmb.2012.02.040
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N-Terminal Domain of Bombyx mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease

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Cited by 120 publications
(123 citation statements)
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“…The fibroin heavy chain consists of the two hydrophilic N- and C-terminal domains (NT and CT), and a highly repetitive glycine and alanine-rich (GA) region consisting of 12 repetitive GA segments with conserved linker sequences in between. The fibroin heavy chain NT (FibNT) is 151 amino acid residues long [33] and adopts mainly a random coil conformation at neutral pH, while it folds into a double-layered anti-parallel beta sheet dimer at low pH [34]. The pH sensitivity is attributed to a cluster of acidic residues that are protonated around pH 6 and thereby the conformational change can take place [34].…”
Section: A Comparison Of Fibroins and Spidroinsmentioning
confidence: 99%
See 1 more Smart Citation
“…The fibroin heavy chain consists of the two hydrophilic N- and C-terminal domains (NT and CT), and a highly repetitive glycine and alanine-rich (GA) region consisting of 12 repetitive GA segments with conserved linker sequences in between. The fibroin heavy chain NT (FibNT) is 151 amino acid residues long [33] and adopts mainly a random coil conformation at neutral pH, while it folds into a double-layered anti-parallel beta sheet dimer at low pH [34]. The pH sensitivity is attributed to a cluster of acidic residues that are protonated around pH 6 and thereby the conformational change can take place [34].…”
Section: A Comparison Of Fibroins and Spidroinsmentioning
confidence: 99%
“…The fibroin heavy chain NT (FibNT) is 151 amino acid residues long [33] and adopts mainly a random coil conformation at neutral pH, while it folds into a double-layered anti-parallel beta sheet dimer at low pH [34]. The pH sensitivity is attributed to a cluster of acidic residues that are protonated around pH 6 and thereby the conformational change can take place [34]. The fibroin heavy chain CT (FibCT) is 58 residues long, its structure has not been characterized, and it is bound to the light chain by a disulfide bond.…”
Section: A Comparison Of Fibroins and Spidroinsmentioning
confidence: 99%
“…In general, silk processing in silk glands of spiders shows similarities to the process in silkworms. The protein solutions are highly concentrated, a drop in pH induces oligomerisation of the spidroins controlled by the terminal domains (which reveal five helix bundles in the case of spider silk proteins [33,34]), and ions are added prior to the final fibre formation [35].…”
Section: Natural Silk Processingmentioning
confidence: 99%
“…However, the hydrophilic spacers are acidic as are the N-terminal head group and the C-terminally bound light chain of SF, leading to a negative net charge at neutral pH and as reflected by an isoelectric point (pI) of about 4 [4,60]. The role of the N-terminal domain is particularly well documented for the pH-dependent control of fiber formation, preventing premature formation of b-sheets at neutral pH and guiding fiber formation during acidification [61][62][63] and has been reviewed before [64,65]. The role of the C-terminus includes influence on both, storage and ordered assembly [66,67].…”
Section: Phmentioning
confidence: 99%