Pheromone binding protein: Difference between revisions

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==Introduction==
==Introduction==
<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of ''Apis mellifera'' scene=''>
<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of ''Apis mellifera'' scene=''>
Pheromone binding proteins [http://en.wikipedia.org/wiki/Pheromone_binding_protein (PBP)] are type of Odorant binding proteins [http://en.wikipedia.org/wiki/Odorant-binding_protein (OBP)] - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates  
Pheromone binding proteins [http://en.wikipedia.org/wiki/Pheromone_binding_protein (PBP)] are type of Odorant binding proteins [http://en.wikipedia.org/wiki/Odorant-binding_protein (OBP)] - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates<ref>DOI:10.3389/fphys.2014.00320</ref>.
<ref>DOI:10.3389/fphys.2014.00320</ref>.
The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.  
The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.  
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.


== Pheromone-binding protein ASP1 ==
== Pheromone-binding protein ASP1 ==


Chemical communication is crucial in social insects, where a complicated and delicate system of signals must be maintained in order to preserve the fragile equilibrium between the queen and the workers.
Chemical communication is crucial in social insects, where a complicated and delicate system of signals must be maintained in order to preserve the fragile equilibrium between the queen and the workers. In the hive of the honey bee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] this equilibrium exists partially due to the extraction of blend of substances called queen mandibular pheromone [http://en.wikipedia.org/wiki/Honey_bee_pheromones#Queen_mandibular_pheromone (QMP)], by the queen <ref>Winston, M.L., 1987. The Biology of the Honey Bee. Harvard University Press, Cambridge, MA.</ref>. The three major component of the QMP blend are: 9-keto-2(E)-decenoic acid (9-ODA) and 9-hydroxy-2(E)-decenoic acid (9-HDA R-(−) or S-(+)).     
In the hive of the honey bee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] this equilibrium exists partially due to the extraction of blend of substances called queen mandibular pheromone [http://en.wikipedia.org/wiki/Honey_bee_pheromones#Queen_mandibular_pheromone (QMP)], by the queen <ref>Winston, M.L., 1987. The Biology of the Honey Bee. Harvard University Press, Cambridge, MA.</ref>. The three major component of the QMP blend are: 9-keto-2(E)-decenoic acid (9-ODA) and 9-hydroxy-2(E)-decenoic acid (9-HDA R-(−) or S-(+)).     
Pheromone-binding protein [http://www.uniprot.org/uniprot/Q9U9J6/ ASP] of the honeybee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] L. (Hymenoptera: Apidea) was first isolated and characterized by Danty ''et al''. (1998)<ref>DOI:10.1016/j.jmb.2008.04.048</ref> from the bee antennae.  
Pheromone-binding protein [http://www.uniprot.org/uniprot/Q9U9J6/ ASP] of the honeybee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] L. (Hymenoptera: Apidea) was first isolated and characterized by Danty ''et al''. (1998)<ref>DOI:10.1016/j.jmb.2008.04.048</ref> from the bee antennae.  
Pheromone-binding protein [http://www.uniprot.org/uniprot/Q9U9J6/ ASP] of the honeybee [http://en.wikipedia.org/wiki/Apis_mellifera ''Apis mellifera''] L. (Hymenoptera: Apidea) was first isolated and characterized by Danty ''et al''. (1998)<ref>DOI:10.1016/j.jmb.2008.04.048</ref> from the bee antennae.


== Structure ==
== Structure ==
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== Interaction with the ligand 9-ODA==
== Interaction with the ligand 9-ODA==
<scene name='60/609542/9-oda/3'>9-ODA</scene>
<scene name='60/609542/9-oda/3'>9-ODA</scene>
The carboxyl end of the component 9-ODA points towards the solvent, and has no any interaction with residues of the protein. The residues in the binding site are <scene name='60/609542/Binding_site/3'>hydrophobic</scene>
The component 9-ODA is binding to the binding site with a <scene name='60/609542/Glycerol/2'>glycerol molecule</scene>.
The carboxyl end of 9-ODA points towards the solvent, and has no bonds with residues of the protein. The residues in the binding site are <scene name='60/609542/Binding_site/3'>hydrophobic</scene>
, and the connection between 9-ODA and ASP1 involve hydrogen bonds.
, and the connection between 9-ODA and ASP1 involve hydrogen bonds.
----
<scene name='60/609542/Glycerol/2'>Glycerol</scene>




== References ==
== References ==
<references/>
<references/>

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