scholarly journals Ligand binding and homology modelling of insect odorant-binding proteins

2014 ◽  
Vol 39 (3) ◽  
pp. 183-198 ◽  
Author(s):  
Herbert Venthur ◽  
Ana Mutis ◽  
Jing-Jiang Zhou ◽  
Andrés Quiroz
Keyword(s):  
Ligand Binding ◽  
Binding Proteins ◽  
Homology Modelling ◽  
Odorant Binding Proteins ◽  
Odorant Binding

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

Probe-dependence of competitive fluorescent ligand binding assays to odorant-binding proteins

2019 ◽  
Vol 412 (3) ◽  
pp. 547-554 ◽  
Author(s):  
Jiajun Tan ◽  
Valeriia Zaremska ◽  
Sierin Lim ◽  
Wolfgang Knoll ◽  
Paolo Pelosi
Keyword(s):  
Ligand Binding ◽  
Binding Proteins ◽  
Binding Assays ◽  
Odorant Binding Proteins ◽  
Odorant Binding ◽  
Fluorescent Ligand

Subtypes of odorant-binding proteins. Heterologous expression and ligand binding

1998 ◽  
Vol 254 (2) ◽  
pp. 318-324 ◽  
Author(s):  
Dietrich Lobel ◽  
Silvana Marchese ◽  
Jurgen Krieger ◽  
Paolo Pelosi ◽  
Heinz Breer
Keyword(s):  
Ligand Binding ◽  
Heterologous Expression ◽  
Binding Proteins ◽  
Odorant Binding Proteins ◽  
Odorant Binding

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1574 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Denis O. Roginskii ◽  
Olesya V. Stepanenko ◽  
Irina M. Kuznetsova ◽  
Vladimir N. Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

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