1obp

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(New page: 200px<br /><applet load="1obp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obp, resolution 2.00&Aring;" /> '''ODORANT-BINDING PROT...)
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[[Image:1obp.gif|left|200px]]<br /><applet load="1obp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1obp, resolution 2.00&Aring;" />
caption="1obp, resolution 2.00&Aring;" />
'''ODORANT-BINDING PROTEIN FROM BOVINE NASAL MUCOSA'''<br />
'''ODORANT-BINDING PROTEIN FROM BOVINE NASAL MUCOSA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1OBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with UNX as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBP OCA].
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1OBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBP OCA].
==Reference==
==Reference==
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:53:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:47 2008''

Revision as of 12:15, 21 February 2008


1obp, resolution 2.00Å

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ODORANT-BINDING PROTEIN FROM BOVINE NASAL MUCOSA

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

1OBP is a Single protein structure of sequence from Bos taurus with as ligand. 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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