A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP. Gell, D., Westman, B., Gorman, D., Liew, C., Welch, J., Weiss, M., & Mackay, J. Journal of Molecular Biology, 362(2):287-297, 2006. doi abstract bibtex The 22 kDa haem-binding protein, p22HBP, is highly expressed in erythropoietic tissues and binds to a range of metallo- and non-metalloporphyrin molecules with similar affinities, suggesting a role in haem regulation or synthesis. We have determined the three-dimensional solution structure of p22HBP and mapped the porphyrin-binding site, which comprises a number of loops and a α-helix all located on a single face of the molecule. The structure of p22HBP is related to the bacterial multi-drug resistance protein BmrR, and is the first protein with this fold to be identified in eukaryotes. Strikingly, the porphyrin-binding site in p22HBP is located in a similar position to the drug-binding site of BmrR. These similarities suggest that the broad ligand specificity observed for both BmrR and p22HBP may result from a conserved ligand interaction mechanism. Taken together, these data suggest that the both the fold and its associated function, that of binding to a broad range of small hydrophobic molecules, are ancient, and have been adapted throughout evolution for a variety of purposes. © 2006 Elsevier Ltd. All rights reserved.
@article{
title = {A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP},
type = {article},
year = {2006},
pages = {287-297},
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abstract = {The 22 kDa haem-binding protein, p22HBP, is highly expressed in erythropoietic tissues and binds to a range of metallo- and non-metalloporphyrin molecules with similar affinities, suggesting a role in haem regulation or synthesis. We have determined the three-dimensional solution structure of p22HBP and mapped the porphyrin-binding site, which comprises a number of loops and a α-helix all located on a single face of the molecule. The structure of p22HBP is related to the bacterial multi-drug resistance protein BmrR, and is the first protein with this fold to be identified in eukaryotes. Strikingly, the porphyrin-binding site in p22HBP is located in a similar position to the drug-binding site of BmrR. These similarities suggest that the broad ligand specificity observed for both BmrR and p22HBP may result from a conserved ligand interaction mechanism. Taken together, these data suggest that the both the fold and its associated function, that of binding to a broad range of small hydrophobic molecules, are ancient, and have been adapted throughout evolution for a variety of purposes. © 2006 Elsevier Ltd. All rights reserved.},
bibtype = {article},
author = {Gell, D.A. and Westman, B.J. and Gorman, D. and Liew, C. and Welch, J.J. and Weiss, M.J. and Mackay, J.P.},
doi = {10.1016/j.jmb.2006.07.010},
journal = {Journal of Molecular Biology},
number = {2}
}
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