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10.1038/s41598-017-05084-8 http://scihub22266oqcxt.onion/10.1038/s41598-017-05084-8 C5504011!5504011 !28694495     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28694495 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2017 ; 7 (1 ): 4932 Nephropedia Template TP {{tp|p=28694495 |t=2017. Functional determinants of protein assembly into homomeric complexes |pdf=|usr=}}{{28694495 }} gab.com Text Functional determinants of protein assembly into homomeric complexes JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28694495 #FOAvip Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure. Twit Text FOAVip Functional determinants of protein assembly into homomeric complexes ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28694495 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28694495 #FOAvip English Wikipedia <ref>{{Cite pmid|28694495 }}</ref> Functional determinants of protein assembly into homomeric complexes #MMPMID28694495 Bergendahl LT ; Marsh JA Sci Rep 2017[Jul]; 7 (1 ): 4932 PMID28694495 show ga Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure. |*Protein Multimerization [MESH] |Humans [MESH] |Models, Molecular [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Protein Interaction Domains and Motifs [MESH]Functional determinants of protein assembly into homomeric complexes (epmc).pdf DeepDyve Pubget Overpricing