4zpy
From Proteopedia
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zpy OCA], [http://pdbe.org/4zpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zpy RCSB], [http://www.ebi.ac.uk/pdbsum/4zpy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zpy ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zpy OCA], [http://pdbe.org/4zpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zpy RCSB], [http://www.ebi.ac.uk/pdbsum/4zpy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zpy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Recent studies reveal that the mechanical properties of virus particles may have been shaped by evolution to facilitate virus survival. Manipulation of the mechanical behavior of virus capsids is leading to a better understanding of viral infection, and to the development of virus-based nanoparticles with improved mechanical properties for nanotechnological applications. In the minute virus of mice (MVM), deleterious mutations around capsid pores involved in infection-related translocation events invariably increased local mechanical stiffness and interfered with pore-associated dynamics. To provide atomic-resolution insights into biologically relevant changes in virus capsid mechanics, we have determined by X-ray crystallography the structural effects of deleterious, mechanically stiffening mutations around the capsid pores. Data show that the cavity-creating N170A mutation at the pore wall does not induce any dramatic structural change around the pores, but instead generates subtle rearrangements that propagate throughout the capsid, resulting in a more compact, less flexible structure. Analysis of the spacefilling L172W mutation revealed the same relationship between increased stiffness and compacted capsid structure. Implications for understanding connections between virus mechanics, structure, dynamics and infectivity, and for engineering modified virus-based nanoparticles, are discussed. | ||
+ | |||
+ | Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.,Guerra P, Valbuena A, Querol-Audi J, Silva C, Castellanos M, Rodriguez-Huete A, Garriga D, Mateu MG, Verdaguer N Sci Rep. 2017 Jun 22;7(1):4101. doi: 10.1038/s41598-017-04345-w. PMID:28642465<ref>PMID:28642465</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4zpy" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 11:33, 3 August 2017
Structure of N170A MVM mutant empty capsid
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