1GM6

3-D STRUCTURE OF A SALIVARY LIPOCALIN FROM BOAR

1GM6 の概要

• エントリーDOI: 10.2210/pdb1gm6/pdb
• 分子名称: SALIVARY LIPOCALIN, CADMIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: odorant-binding protein
• 由来する生物種: SUS SCROFA (PIG)
• 細胞内の位置: Secreted: P81608
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20367.14

構造登録者

Spinelli, S.,Vincent, F.,Pelosi, P.,Tegoni, M.,Cambillau, C. (登録日: 2001-09-11, 公開日: 2002-05-30, 最終更新日: 2024-11-13)

主引用文献

Spinelli, S.,Vincent, F.,Pelosi, P.,Tegoni, M.,Cambillau, C.
Boar Salivary Lipocalin. Three-Dimensional X-Ray Structure and Androsterol/Androstenone Docking Simulations.
Eur.J.Biochem., 269:2449-, 2002

PubMed Abstract: The X-ray structure of variant A of authentic boar salivary lipocalin (SAL), a pheromone-binding protein specifically expressed in the submaxillary glands of the boar, has been solved and refined at 2.1 A resolution. The structure displays a classical lipocalin fold with a nine-stranded sandwiched beta barrel and an alpha helix. A putative glycosylation site, at position 53, has been found to carry a GlcNAc sugar residue. In contrast with what was expected on the basis of mass spectroscopy reports, the internal cavity was found to be devoid of bound pheromonal compound (androstenone or androstenol). Instead, a small electron density volume could be satisfied by a glycerol molecule, a component of the cryoprotecting liquor. The internal cavity was revealed to be very small for steroid compound accommodation. Therefore, docking and molecular dynamics experiments were performed with both pheromonal compounds. These simulations clearly demonstrate a volume increase of the cavity upon steroid binding and the adaptation of the amino-acid side chains to the steroid molecules. This explains the higher affinity of SAL for both steroid molecules compared to other smaller molecules, although no specific interaction is established with either compound.

PubMed: 12027882
DOI: 10.1046/J.1432-1033.2002.02901.X

実験手法

X-RAY DIFFRACTION (2.13 Å)