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PDBsum entry 1a3y
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism.
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Authors
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S.Spinelli,
R.Ramoni,
S.Grolli,
J.Bonicel,
C.Cambillau,
M.Tegoni.
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Ref.
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Biochemistry, 1998,
37,
7913-7918.
[DOI no: ]
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PubMed id
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Abstract
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The X-ray structure of the porcine odorant binding protein (OBPp) was determined
at 2.25 A resolution. This lipocalin is a monomer and is devoid of naturally
occurring bound ligand, contrary to what was observed in the case of bovine OBP
[Tegoni, M., et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet, M. A., et
al. (1996) Nat. Struct. Biol. 3, 934-939]. In this latter protein, a dimer
without any disulfide bridges, domain swapping was found to occur between the
beta- and alpha-domains. A single Gly (121) insertion was found in OBPp when it
was compared to OBPb, which may prevent domain swapping from taking place. The
presence of a disulfide bridge between the OBPp beta- and alpha-domains
(cysteines 63 and 155) may lock the resulting fold in a nonswapped monomeric
conformation. Comparisons with other OBPs indicate that the two cysteines
involved in the OBPp disulfide bridge are conserved in the sequence, suggesting
that OBPp may be considered a prototypic OBP fold, and not OBPb.
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Secondary reference #1
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Title
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Affinities of nutty and green-Smelling pyrazines and thiazoles to odorant-Binding proteins, In relation with their lipophilicity.
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Authors
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M.F.Hérent,
S.Collin,
P.Pelosi.
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Ref.
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Chem Senses, 1995,
20,
601-608.
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PubMed id
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Secondary reference #2
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Title
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Binding of selected odorant to bovine and porcine odorant-Binding proteins
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Authors
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M.D.Monte,
M.Centini,
C.Anselmi,
P.Pelosi.
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Ref.
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chem senses, 1993,
18,
713.
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Secondary reference #3
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Title
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Purification and characterization of two odorant-Binding proteins from nasal tissue of rabbit and pig.
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Authors
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M.Dal monte,
I.Andreini,
R.Revoltella,
P.Pelosi.
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Ref.
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Comp Biochem Physiol B, 1991,
99,
445-451.
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PubMed id
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