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10.1073/pnas.0402992101 http://scihub22266oqcxt.onion/10.1073/pnas.0402992101 15289612!511008!15289612     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\15289612.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2004 ; 101 (32): 11628-33 Nephropedia Template TP {{tp|p=15289612|t=2004. The structure of human parvovirus B19 |pdf=|usr=}}{{15289612}} gab.com Text The structure of human parvovirus B19 JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=15289612 #FOAvip Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C(alpha) atoms can be aligned structurally with a rms deviation of 1.8 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region. Twit Text FOAVip The structure of human parvovirus B19 ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=15289612 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=15289612 #FOAvip English Wikipedia <ref>{{Cite pmid|15289612}}</ref> The structure of human parvovirus B19 #MMPMID15289612 Kaufmann B; Simpson AA; Rossmann MG Proc Natl Acad Sci U S A 2004[Aug]; 101 (32): 11628-33 PMID15289612show ga Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C(alpha) atoms can be aligned structurally with a rms deviation of 1.8 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region. |*Crystallography, X-Ray[MESH] |Capsid Proteins/*chemistry[MESH] |Humans[MESH] |Models, Molecular[MESH] |Parvovirus B19, Human/*chemistry[MESH] |Protein Conformation[MESH] |Sequence Alignment[MESH] |Surface Properties[MESH]The structure of human parvovirus B19 (epmc).pdf DeepDyve Pubget Overpricing