1gm6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The X-ray structure of variant A of authentic boar salivary lipocalin | + | 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== | ==About this Structure== | ||
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[[Category: salivary lipocalin]] | [[Category: salivary lipocalin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:34 2008'' |
Revision as of 10:51, 21 February 2008
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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 , and as ligands. Known structural/functional Site: . 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 Thu Feb 21 12:51:34 2008
Categories: Single protein | Sus scrofa | Cambillau, C. | Pelosi, P. | Spinelli, S. | Tegoni, M. | Vincent, F. | CD | GOL | NAG | Odorant binding protein | Salivary lipocalin
