کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2189076 | 1096196 | 2006 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP A Novel Haem-binding Interface in the 22 kDa Haem-binding Protein p22HBP](/preview/png/2189076.png)
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.
Journal: Journal of Molecular Biology - Volume 362, Issue 2, 15 September 2006, Pages 287–297