1pbo

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbo OCA], [http://www.ebi.ac.uk/pdbsum/1pbo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pbo RCSB]</span>
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[[Category: Bianchet, M A.]]
[[Category: Bianchet, M A.]]
[[Category: Monaco, H.]]
[[Category: Monaco, H.]]
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[[Category: SES]]
 
[[Category: lipocalin]]
[[Category: lipocalin]]
[[Category: odorant-binding]]
[[Category: odorant-binding]]
[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:36 2008''

Revision as of 19:57, 30 March 2008


PDB ID 1pbo

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF BOVINE ODORANT BINDING PROTEIN (OBP) WITH A SELENIUM CONTAINING ODORANT


Overview

Odorant binding protein (OBP) is the major odorant binding component of mammalian nasal mucosa. The two structures of bovine OBP reported in this paper (one crystallized as purified and one soaked in the presence of a selenium-containing odorant) show that: (i) the OBP dimer is composed of two compact domains related by an approximate two-fold axis of symmetry; (ii) between residues 122 and 123 the polypeptide chains cross from one domain to the other such that each domain is formed by residues from both monomers; (iii) purified OBP already contains two bound odorant molecules (one per monomer)-odorant binding occurs by replacement of these molecules with the added odorant; and (iv) the structure of the odorant binding site can explain OBP's extraordinarily broad odorant specificity.

About this Structure

1PBO is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition., Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM, Nat Struct Biol. 1996 Nov;3(11):934-9. PMID:8901871

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