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10.1042/BST20150082 http://scihub22266oqcxt.onion/10.1042/BST20150082 C4613516!4613516!26517891     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Soc+Trans 2015 ; 43 (5): 838-43 Nephropedia Template TP {{tp|p=26517891|t=2015. The centriolar protein CPAP G-box: an amyloid fibril in a single domain |pdf=|usr=}}{{26517891}} gab.com Text The centriolar protein CPAP G-box: an amyloid fibril in a single domain JO: Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=26517891 #FOAvip Centrioles are evolutionarily conserved cylindrical cell organelles with characteristic radial symmetry. Despite their considerable size (400 nm × 200 nm, in humans), genetic studies suggest that relatively few protein components are involved in their assembly. We recently characterized the molecular architecture of the centrosomal P4.1-associated protein (CPAP), which is crucial for controlling the centriolar cylinder length. Here, we review the remarkable architecture of the C-terminal domain of CPAP, termed the G-box, which comprises a single, entirely solvent exposed, antiparallel ?-sheet. Molecular dynamics simulations support the stability of the G-box domain even in the face of truncations or amino acid substitutions. The similarity of the G-box domain to amyloids (or amyloid precursors) is strengthened by its oligomeric arrangement to form continuous fibrils. G-box fibrils were observed in crystals as well as in solution and are also supported by simulations. We conclude that the G-box domain may well represent the best analogue currently available for studies of exposed ?-sheets, unencumbered by additional structural elements or severe aggregations problems. Twit Text FOAVip The centriolar protein CPAP G-box: an amyloid fibril in a single domain ????Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=26517891 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26517891 #FOAvip English Wikipedia <ref>{{Cite pmid|26517891}}</ref> The centriolar protein CPAP G-box: an amyloid fibril in a single domain #MMPMID26517891 Cutts E; Inglis A; Stansfeld P; Vakonakis I; Hatzopoulos G Biochem Soc Trans 2015[Oct]; 43 (5): 838-43 PMID26517891show ga Centrioles are evolutionarily conserved cylindrical cell organelles with characteristic radial symmetry. Despite their considerable size (400 nm × 200 nm, in humans), genetic studies suggest that relatively few protein components are involved in their assembly. We recently characterized the molecular architecture of the centrosomal P4.1-associated protein (CPAP), which is crucial for controlling the centriolar cylinder length. Here, we review the remarkable architecture of the C-terminal domain of CPAP, termed the G-box, which comprises a single, entirely solvent exposed, antiparallel ?-sheet. Molecular dynamics simulations support the stability of the G-box domain even in the face of truncations or amino acid substitutions. The similarity of the G-box domain to amyloids (or amyloid precursors) is strengthened by its oligomeric arrangement to form continuous fibrils. G-box fibrils were observed in crystals as well as in solution and are also supported by simulations. We conclude that the G-box domain may well represent the best analogue currently available for studies of exposed ?-sheets, unencumbered by additional structural elements or severe aggregations problems. äThe centriolar protein CPAP G-box: an amyloid fibril in a single domai(epmc).pdf DeepDyve Pubget Overpricing