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Correction

Correction: The Five-To-Six-Coordination Transition of Ferric Human Serum Heme-Albumin Is Allosterically-Modulated by Ibuprofen and Warfarin: A Combined XAS and MD Study

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Fig. 5 is incorrect. Please see the corrected Fig. 5 here.

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Fig 5. Conformational transition of HSA-heme-Fe(III) upon ligand binding to the FA2 site.

Panel A. Three-dimensional representation of the starting crystal structure (cyan, PDB entry 1O9X [22]) of HSA-heme-Fe(III). Heme-Fe(III) and the His146 and Tyr161 residues are highlighted in blue. The Glu131-Arg145 α-helix is represented in magenta. Panel B. Three-dimensional representation of the final model (orange) of HSA-heme-Fe(III) obtained via SMDS. Heme-Fe(III) and the His146 and Tyr161 residues are highlighted in red. The Glu131-Arg145 α-helix is represented in green. Panel C. Superposition of the starting crystal structure and of the final model of HSA-heme-Fe(III). The picture has been drawn using the UCSF Chimera package [67], [68].

https://doi.org/10.1371/journal.pone.0123144.g001

Reference

  1. 1. Meneghini C, Leboffe L, Bionducci M, Fanali G, Meli M, Colombo G, et al. (2014) The Five-To-Six-Coordination Transition of Ferric Human Serum Heme-Albumin Is Allosterically-Modulated by Ibuprofen and Warfarin: A Combined XAS and MD Study. PLoS ONE 9(8): e104231. pmid:25153171

Citation: The PLOS ONE Staff (2015) Correction: The Five-To-Six-Coordination Transition of Ferric Human Serum Heme-Albumin Is Allosterically-Modulated by Ibuprofen and Warfarin: A Combined XAS and MD Study. PLoS ONE 10(3): e0123144. https://doi.org/10.1371/journal.pone.0123144

Published: March 31, 2015

Copyright: © 2015 The PLOS ONE Staff. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited