1al2

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1al2, resolution 2.9Å

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P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT V1160I

Overview

In 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.

About this Structure

1AL2 is a Protein complex structure of sequences from Human poliovirus 1 with MYR and SPH as ligands. Full crystallographic information is available from OCA.

Reference

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

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