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10.1038/nature15381 http://scihub22266oqcxt.onion/10.1038/nature15381 C4886846!4886846!26416747     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nature 2015 ; 526 (7571): 140-3 Nephropedia Template TP {{tp|p=26416747|t=2015. In situ structural analysis of the human nuclear pore complex |pdf=|usr=}}{{26416747}} gab.com Text In situ structural analysis of the human nuclear pore complex JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=26416747 #FOAvip Nuclear pore complexes (NPCs) are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Elucidating their 110 MDa structure imposes a formidable challenge and requires in situ structural biology approaches. Fifteen out of about thirty nucleoporins (Nups) are structured and form the Y- and inner ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central channel of ?60 nm in diameter 1. The scaffold is decorated with transport channel Nups that often contain phenylalanine (FG)-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y-complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here, we combined cryo electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modeling to generate the most comprehensive architectural model of the NPC to date. Our data suggest previously unknown protein interfaces across Y-complexes and to inner ring complex members. We demonstrate that the higher eukaryotic transport channel Nup358 (RanBP2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and transport channel Nups. We conclude that, similarly to coated vesicles, multiple copies of the same structural building block - although compositionally identical - engage in different local sets of interactions and conformations. Twit Text FOAVip In situ structural analysis of the human nuclear pore complex ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=26416747 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26416747 #FOAvip English Wikipedia <ref>{{Cite pmid|26416747}}</ref> In situ structural analysis of the human nuclear pore complex #MMPMID26416747 von Appen A; Kosinski J; Sparks L; Ori A; DiGuilio AL; Vollmer B; Mackmull MT; Banterle N; Parca L; Kastritis P; Buczak K; Mosalaganti S; Hagen W; Andres-Pons A; Lemke EA; Bork P; Antonin W; Glavy JS; Bui KH; Beck M Nature 2015[Oct]; 526 (7571): 140-3 PMID26416747show ga Nuclear pore complexes (NPCs) are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Elucidating their 110 MDa structure imposes a formidable challenge and requires in situ structural biology approaches. Fifteen out of about thirty nucleoporins (Nups) are structured and form the Y- and inner ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central channel of ?60 nm in diameter 1. The scaffold is decorated with transport channel Nups that often contain phenylalanine (FG)-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y-complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here, we combined cryo electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modeling to generate the most comprehensive architectural model of the NPC to date. Our data suggest previously unknown protein interfaces across Y-complexes and to inner ring complex members. We demonstrate that the higher eukaryotic transport channel Nup358 (RanBP2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and transport channel Nups. We conclude that, similarly to coated vesicles, multiple copies of the same structural building block - although compositionally identical - engage in different local sets of interactions and conformations. äIn situ structural analysis of the human nuclear pore complex (epmc).pdf DeepDyve Pubget Overpricing