Journal:Acta Cryst D:S2059798322007677
From Proteopedia
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Our studies conclude that the increased affinity of the Q498Y RBD protein is due to a higher number and types of inter-molecular interactions provided by the RBD tyrosine 498 side chain, compared to those associated to glutamine 498 in the wild-type RBD. Comparison of the interatomic contacts between RBD and ACE2 in the wild type and Q498Y structures: | Our studies conclude that the increased affinity of the Q498Y RBD protein is due to a higher number and types of inter-molecular interactions provided by the RBD tyrosine 498 side chain, compared to those associated to glutamine 498 in the wild-type RBD. Comparison of the interatomic contacts between RBD and ACE2 in the wild type and Q498Y structures: | ||
*<scene name='91/918482/Cv/10'>Interatomic polar interactions</scene> are shown as white dashed lines. The cut-off for Van der Waals and H-bonds are set to 4 Å and 3.4 Å, respectively. Interacting residues are depicted as sticks. | *<scene name='91/918482/Cv/10'>Interatomic polar interactions</scene> are shown as white dashed lines. The cut-off for Van der Waals and H-bonds are set to 4 Å and 3.4 Å, respectively. Interacting residues are depicted as sticks. | ||
| + | <jmol><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only wild type structure</text></jmolButton><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only Q498Y structure</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both wild type and Q498Y</text></jmolButton></jmol> | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:58, 2 August 2022
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