Summary for 2HVA
| Entry DOI | 10.2210/pdb2hva/pdb |
| Descriptor | Heme-binding protein 1 (1 entity in total) |
| Functional Keywords | haem-binding protein, beta-beta-alpha-beta-beta repeat, hydrophobic-ligand binding domain, ligand binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm: Q9R257 |
| Total number of polymer chains | 1 |
| Total formula weight | 21218.91 |
| Authors | Gell, D.A.,Mackay, J.P.,Westman, B.J.,Liew, C.K.,Gorman, D. (deposition date: 2006-07-28, release date: 2006-08-08, Last modification date: 2024-05-29) |
| Primary citation | Gell, D.A.,Westman, B.J.,Gorman, D.,Liew, C.K.,Welch, J.J.,Weiss, M.J.,Mackay, J.P. A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP. J.Mol.Biol., 362:287-297, 2006 Cited by PubMed 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 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. PubMed: 16905148DOI: 10.1016/j.jmb.2006.07.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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