1dzk: Difference between revisions

Revision as of 23:53, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dzk.png

Template:STRUCTURE 1dzk

PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH PYRAZINE (2-ISOBUTYL-3-METOXYPYRAZINE)PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH PYRAZINE (2-ISOBUTYL-3-METOXYPYRAZINE)

Template:ABSTRACT PUBMED 10864504

About this StructureAbout this Structure

1DZK is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes., Vincent F, Spinelli S, Ramoni R, Grolli S, Pelosi P, Cambillau C, Tegoni M, J Mol Biol. 2000 Jun 30;300(1):127-39. PMID:10864504

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH PYRAZINE (2-ISOBUTYL-3-METOXYPYRAZINE)'''
+===PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH PYRAZINE (2-ISOBUTYL-3-METOXYPYRAZINE)===
-==Overview==
+<!--
-Porcine odorant binding protein (pOBP) is a monomer of 157 amino acid residues, purified in abundance from pig nasal mucosa. In contrast to the observation on lipocalins as retinol binding protein (RBP), major urinary protein (MUP) or bovine odorant binding protein (bOBP), no naturally occurring ligand was found in the beta-barrel cavity of pOBP. Porcine OBP was therefore chosen as a simple model for structure/function studies with odorant molecules. In competition experiments with tritiated pyrazine, the affinity of pOBP towards several odorant molecules belonging to different chemical classes has been found to be of the micromolar order, with a 1:1 stoichiometry. The X-ray structures of pOBP complexed to these molecules were determined at resolution between 2.15 and 1.4 A. As expected, the electron density of the odorant molecules was observed into the hydrophobic beta-barrel of the lipocalin. Inside this cavity, very few specific interactions were established between the odorant molecule and the amino acid side-chains, which did not undergo significant conformational change. The high B-factors observed for the odorant molecules as well as the existence of alternative conformations reveal a non-specific mode of binding of the odorant molecules in the cavity.
+The line below this paragraph, {{ABSTRACT_PUBMED_10864504}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10864504}}
 ==About this Structure==
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 [[Category: Lipocalin]]
 [[Category: Odorant binding protein]]
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