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10.1016/j.matbio.2016.06.006 http://scihub22266oqcxt.onion/10.1016/j.matbio.2016.06.006 C5338690!5338690!27425256     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Matrix+Biol 2017 ; 57-58 (ä): 204-12 Nephropedia Template TP {{tp|p=27425256|t=2017. Crystallographic analysis of the laminin ?2 short arm reveals how the LF domain is inserted into a regular array of LE domains |pdf=|usr=}}{{27425256}} gab.com Text Crystallographic analysis of the laminin 2 short arm reveals how the LF domain is inserted into a regular array of LE domains JO: Matrix Biol http://www.kidney.de/pget.php?&tw=1&pmid=27425256 #FOAvip Laminins are a major constituent of all basement membranes. The polymerisation of laminins at the cell surface is mediated by the three short arms of the cross-shaped laminin heterotrimer. The short arms contain repeats of laminin-type epidermal growth factor-like (LE) domains, interspersed with globular domains of unknown function. A single LF domain is inserted between LE5 and LE6 of the laminin ?1 and ?2 chains. We report the crystal structure at 1.85 Å resolution of the laminin ?2 LE5-LF-LE6 region. The LF domain consists of a ?-sandwich related to bacterial family 35 carbohydrate binding modules, and more distantly to the L4 domains present in the short arms of laminin ? and ? chains. An ?-helical region mediates the extensive interaction of the LF domain with LE5. The relative arrangement of LE5 and LE6 is very similar to that of consecutive LE domains in uninterrupted LE tandems. Fitting atomic models to a low-resolution structure of the first eight domains of the laminin ?1 chain determined by small-angle X-ray scattering suggests a deviation from the regular LE array at the LE4?LE5 junction. These results advance our understanding of laminin structure. Twit Text FOAVip Crystallographic analysis of the laminin 2 short arm reveals how the LF domain is inserted into a regular array of LE domains ????Matrix Biol http://www.kidney.de/pget.php?&tw=1&pmid=27425256 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27425256 #FOAvip English Wikipedia <ref>{{Cite pmid|27425256}}</ref> Crystallographic analysis of the laminin ?2 short arm reveals how the LF domain is inserted into a regular array of LE domains #MMPMID27425256 Pulido D; Briggs DC; Hua J; Hohenester E Matrix Biol 2017[Jan]; 57-58 (ä): 204-12 PMID27425256show ga Laminins are a major constituent of all basement membranes. The polymerisation of laminins at the cell surface is mediated by the three short arms of the cross-shaped laminin heterotrimer. The short arms contain repeats of laminin-type epidermal growth factor-like (LE) domains, interspersed with globular domains of unknown function. A single LF domain is inserted between LE5 and LE6 of the laminin ?1 and ?2 chains. We report the crystal structure at 1.85 Å resolution of the laminin ?2 LE5-LF-LE6 region. The LF domain consists of a ?-sandwich related to bacterial family 35 carbohydrate binding modules, and more distantly to the L4 domains present in the short arms of laminin ? and ? chains. An ?-helical region mediates the extensive interaction of the LF domain with LE5. The relative arrangement of LE5 and LE6 is very similar to that of consecutive LE domains in uninterrupted LE tandems. Fitting atomic models to a low-resolution structure of the first eight domains of the laminin ?1 chain determined by small-angle X-ray scattering suggests a deviation from the regular LE array at the LE4?LE5 junction. These results advance our understanding of laminin structure. äCrystallographic analysis of the laminin ?2 short arm reveals how the (epmc).pdf DeepDyve Pubget Overpricing