1hqp
From Proteopedia
(New page: 200px<br /><applet load="1hqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqp, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1hqp.jpg|left|200px]]<br /><applet load="1hqp" size=" | + | [[Image:1hqp.jpg|left|200px]]<br /><applet load="1hqp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hqp, resolution 2.3Å" /> | caption="1hqp, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF A TRUNCATED FORM OF PORCINE ODORANT-BINDING PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF A TRUNCATED FORM OF PORCINE ODORANT-BINDING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The odorant-binding proteins (OBPs) are a family of structurally related | + | The odorant-binding proteins (OBPs) are a family of structurally related molecules that are found in high concentrations in the nasal mucus of vertebrates and bind with moderate affinity a large family of hydrophobic odorants. On the basis of their quaternary structure, the OBPs have been classified as monomers, homodimers, and heterodimers. Porcine OBP was believed for a long time to be a monomer under physiological conditions but there are recent data that support the existence of a monomer-dimer equilibrium. We have determined the crystal structure of a monoclinic form of porcine OBP and found that the truncated molecules, which lack the first 8 amino acids, pack in the cell as dimers that appear to have physiological relevance. The presence in the maps of electron density for an endogenous ligand has also let us identify the side chain of the amino acids that are at the ligand-binding site. In addition, an alternative way of access to the central cavity that binds the ligands is suggested by the particular packing of the molecules in this unit cell. Proteins 2001;42:201-209. |
==About this Structure== | ==About this Structure== | ||
| - | 1HQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with PRZ as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=PRZ:'>PRZ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Giorgio, R | + | [[Category: Giorgio, R Del.]] |
[[Category: Mancia, F.]] | [[Category: Mancia, F.]] | ||
| - | [[Category: Monaco, H | + | [[Category: Monaco, H L.]] |
[[Category: Perduca, M.]] | [[Category: Perduca, M.]] | ||
[[Category: PRZ]] | [[Category: PRZ]] | ||
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[[Category: lipocalin]] | [[Category: lipocalin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:53 2008'' |
Revision as of 11:03, 21 February 2008
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CRYSTAL STRUCTURE OF A TRUNCATED FORM OF PORCINE ODORANT-BINDING PROTEIN
Overview
The odorant-binding proteins (OBPs) are a family of structurally related molecules that are found in high concentrations in the nasal mucus of vertebrates and bind with moderate affinity a large family of hydrophobic odorants. On the basis of their quaternary structure, the OBPs have been classified as monomers, homodimers, and heterodimers. Porcine OBP was believed for a long time to be a monomer under physiological conditions but there are recent data that support the existence of a monomer-dimer equilibrium. We have determined the crystal structure of a monoclinic form of porcine OBP and found that the truncated molecules, which lack the first 8 amino acids, pack in the cell as dimers that appear to have physiological relevance. The presence in the maps of electron density for an endogenous ligand has also let us identify the side chain of the amino acids that are at the ligand-binding site. In addition, an alternative way of access to the central cavity that binds the ligands is suggested by the particular packing of the molecules in this unit cell. Proteins 2001;42:201-209.
About this Structure
1HQP is a Single protein structure of sequence from Sus scrofa with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a truncated form of porcine odorant-binding protein., Perduca M, Mancia F, Del Giorgio R, Monaco HL, Proteins. 2001 Feb 1;42(2):201-9. PMID:11119644
Page seeded by OCA on Thu Feb 21 13:03:53 2008
