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10.1371/journal.pone.0186570 http://scihub22266oqcxt.onion/10.1371/journal.pone.0186570 C5659604!5659604 !29077715     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29077715 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\29077715 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       PLoS+One 2017 ; 12 (10 ): e0186570 Nephropedia Template TP {{tp|p=29077715 |t=2017. Protein dynamics and structural waters in bromodomains |pdf=|usr=}}{{29077715 }} gab.com Text Protein dynamics and structural waters in bromodomains JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29077715 #FOAvip Bromodomains are epigenetic readers of acetylated lysines that are integral parts of histone tails. The 61 bromodomains in humans are structurally highly conserved but specifically bind to widely varying recognition motifs, suggesting that dynamic rather than static factors are responsible for recognition selectivity. To test this hypothesis, the dynamics of the binding sites and structural water molecules of four bromodomains (ATAD2, BAZ2B, BRD2(1) and CREBBP) representing four different subtypes is studied with 1 ?s MD simulations using the RSFF2 force field. The different dynamics of the ZA-loops and BC-loops between the four bromodomains leads to distinct patterns for the opening and closing of the binding pocket. This in turn determines the structural and energetic properties of the structural waters in the binding pocket, suggesting that these waters are not only important for the recognition itself, as has been proposed previously, but also contribute to the selectivity of different bromodomains. Twit Text FOAVip Protein dynamics and structural waters in bromodomains ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29077715 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29077715 #FOAvip English Wikipedia <ref>{{Cite pmid|29077715 }}</ref> Protein dynamics and structural waters in bromodomains #MMPMID29077715 Zhang X ; Chen K ; Wu YD ; Wiest O PLoS One 2017[]; 12 (10 ): e0186570 PMID29077715 show ga Bromodomains are epigenetic readers of acetylated lysines that are integral parts of histone tails. The 61 bromodomains in humans are structurally highly conserved but specifically bind to widely varying recognition motifs, suggesting that dynamic rather than static factors are responsible for recognition selectivity. To test this hypothesis, the dynamics of the binding sites and structural water molecules of four bromodomains (ATAD2, BAZ2B, BRD2(1) and CREBBP) representing four different subtypes is studied with 1 ?s MD simulations using the RSFF2 force field. The different dynamics of the ZA-loops and BC-loops between the four bromodomains leads to distinct patterns for the opening and closing of the binding pocket. This in turn determines the structural and energetic properties of the structural waters in the binding pocket, suggesting that these waters are not only important for the recognition itself, as has been proposed previously, but also contribute to the selectivity of different bromodomains. |Amino Acid Sequence [MESH] |Epigenesis, Genetic [MESH] |Histones/metabolism [MESH] |Humans [MESH] |Molecular Dynamics Simulation [MESH] |Protein Conformation [MESH] |Proteins/chemistry/genetics/*metabolism [MESH]Protein dynamics and structural waters in bromodomains (epmc).pdf DeepDyve Pubget Overpricing