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<script>script /scripts/10/1056673/Fig_6e/2.spt
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hide water; set zshade off</script>
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<text>Mono pH 6.0</text>
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The novel crystal structures of the Cys59Ser and Cys155Ser mutants help to further define the role of the disulfide bond in stabilizing a ligand-free apo conformation that is disfavoured in both mutants. In fact the <scene name='10/1055499/8ov1_8ov2_8vo3/4'>two mutated structures are remarkably similar to the BIA bound WT structure</scene>.
The novel crystal structures of the Cys59Ser and Cys155Ser mutants help to further define the role of the disulfide bond in stabilizing a ligand-free apo conformation that is disfavoured in both mutants. In fact the <scene name='10/1055499/8ov1_8ov2_8vo3/4'>two mutated structures are remarkably similar to the BIA bound WT structure</scene>.

Revision as of 16:29, 10 October 2024

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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