1gm6
From Proteopedia
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3-D STRUCTURE OF A SALIVARY LIPOCALIN FROM BOAR
Overview
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.
About this Structure
1GM6 is a Single protein structure of sequence from Sus scrofa with NAG, CD and GOL as ligands. Structure known Active Site: CAV. Full crystallographic information is available from OCA.
Reference
Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations., Spinelli S, Vincent F, Pelosi P, Tegoni M, Cambillau C, Eur J Biochem. 2002 May;269(10):2449-56. PMID:12027882
Page seeded by OCA on Mon Nov 5 13:41:05 2007
Categories: Single protein | Sus scrofa | Cambillau, C. | Pelosi, P. | Spinelli, S. | Tegoni, M. | Vincent, F. | CD | GOL | NAG | Odorant binding protein | Salivary lipocalin
