1ar9
P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142YP1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn order to better understand the process of cell entry for non-enveloped viruses, we have solved the crystal structures of five poliovirus mutants which can infect cells expressing mutant poliovirus receptors. Four of these structures have been solved from frozen crystals using cryocrystallographic data collection methods. The mutations have a range of structural consequences, from small local perturbations to significant loop rearrangements. All of the mutant viruses are more labile to conversion to an apparent cell entry intermediate, suggesting that these mutant viruses could compensate for the suboptimal receptors by lowering the thermal energy required to undergo the receptor-mediated conformational change. Structural studies of poliovirus mutants that overcome receptor defects.,Wien MW, Curry S, Filman DJ, Hogle JM Nat Struct Biol. 1997 Aug;4(8):666-74. PMID:9253417[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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