2HVA

Solution Structure of the haem-binding protein p22HBP

「2HC6」から置き換えられました

2HVA の概要

• エントリーDOI: 10.2210/pdb2hva/pdb
• 分子名称: Heme-binding protein 1 (1 entity in total)
• 機能のキーワード: haem-binding protein, beta-beta-alpha-beta-beta repeat, hydrophobic-ligand binding domain, ligand binding protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm: Q9R257
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21218.91

構造登録者

Gell, D.A.,Mackay, J.P.,Westman, B.J.,Liew, C.K.,Gorman, D. (登録日: 2006-07-28, 公開日: 2006-08-08, 最終更新日: 2024-05-29)

主引用文献

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

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: 16905148
DOI: 10.1016/j.jmb.2006.07.010

実験手法

SOLUTION NMR