1GT1

Complex of Bovine Odorant Binding Protein with Aminoanthracene and pyrazine

1GT1 の概要

• エントリーDOI: 10.2210/pdb1gt1/pdb
• 関連するPDBエントリー: 1G85 1GT3 1GT4 1GT5 1HN2 1OBP 1PBO
• 分子名称: ODORANT-BINDING PROTEIN, 2-ISOBUTYL-3-METHOXYPYRAZINE, ANTHRACEN-1-YLAMINE, ... (5 entities in total)
• 機能のキーワード: lipocalin, odorant-binding protein
• 由来する生物種: BOS TAURUS (CATTLE)
• 細胞内の位置: Secreted: P07435
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37737.68

構造登録者

Vincent, F.,Ramoni, R.,Spinelli, S.,Grolli, S.,Conti, V.,Cambillau, C.,Tegoni, M. (登録日: 2002-01-10, 公開日: 2003-10-03, 最終更新日: 2023-12-13)

主引用文献

Vincent, F.,Ramoni, R.,Spinelli, S.,Grolli, S.,Tegoni, M.,Cambillau, C.
Crystal Structures of Bovine Odorant-Binding Protein in Complex with Odorant Molecules.
Eur.J.Biochem., 271:3832-, 2004

PubMed Abstract: The structure of bovine odorant-binding protein (bOBP) revealed a striking feature of a dimer formed by domain swapping [Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. & Cambillau, C. (1996) Nat. Struct. Biol.3, 863-867; Bianchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L. & Amzel, L.M. (1996) Nat. Struct. Biol.3, 934-939] and the presence of a naturally occuring ligand [Ramoni, R., Vincent, F., Grolli, S., Conti, V., Malosse, C., Boyer, F.D., Nagnan-Le Meillour, P., Spinelli, S., Cambillau, C. & Tegoni, M. (2001) J. Biol. Chem.276, 7150-7155]. These features led us to investigate the binding of odorant molecules with bOBP in solution and in the crystal. The behavior of odorant molecules in bOBP resembles that observed with porcine OBP (pOBP), although the latter is monomeric and devoid of ligand when purified. The odorant molecules presented K(d) values with bOBP in the micromolar range. Most of the X-ray structures revealed that odorant molecules interact with a common set of residues forming the cavity wall and do not exhibit specific interactions. Depending on the ligand and on the monomer (A or B), a single residue--Phe89--presents alternate conformations and might control cross-talking between the subunits. Crystal data on both pOBP and bOBP, in contrast with binding and spectroscopic studies on rat OBP in solution, reveal an absence of significant conformational changes involving protein loops or backbone. Thus, the role of OBP in signal triggering remains unresolved.

PubMed: 15373829
DOI: 10.1111/J.1432-1033.2004.04315.X

実験手法

X-RAY DIFFRACTION (1.71 Å)