2hva
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(New page: 200px<br /><applet load="2hva" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hva" /> '''Solution Structure of the haem-binding prote...)
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Revision as of 09:53, 21 November 2007
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Solution Structure of the haem-binding protein p22HBP
Overview
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 alpha-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.
About this Structure
2HVA is a Single protein structure of sequence from Mus musculus. This structure superseeds the now removed PDB entry 2HC6. Full crystallographic information is available from OCA.
Reference
A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP., Gell DA, Westman BJ, Gorman D, Liew C, Welch JJ, Weiss MJ, Mackay JP, J Mol Biol. 2006 Sep 15;362(2):287-97. Epub 2006 Aug 14. PMID:16905148
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