Pheromone binding protein: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 3: Line 3:
As the most ancient sense in nature, chemical communication plays a major role in successful mating, host and selection and other essential behaviors.  
As the most ancient sense in nature, chemical communication plays a major role in successful mating, host and selection and other essential behaviors.  
This becomes 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.   
This becomes 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 (QMP). 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 proteins are soluble proteins invovled in the early stages of pheromone detection.
Pheromone binding proteins are soluble proteins invovled in the early stages of pheromone detection.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee.

Revision as of 17:16, 19 November 2014

IntroductionIntroduction

As the most ancient sense in nature, chemical communication plays a major role in successful mating, host and selection and other essential behaviors.

This becomes 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 Apis mellifera this equilibrium exists partially due to the extraction of blend of substances called queen mandibular pheromone (QMP). 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 proteins are soluble proteins invovled in the early stages of pheromone detection.

As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee.




Pheromone-binding protein ASP of the honeybee Apis mellifera L. (Hymenoptera: Apidea) was first isolated and characterized by Danty et al. (1998)[1] from the bee antennae.

or to the article describing Jmol [2] to the rescue.

Structure

The protein has a .

Full crystallographic information is available from OCA.

Function

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Pheromone binding protein of

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C. Structural basis of the honey bee PBP pheromone and pH-induced conformational change. J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083 doi:10.1016/j.jmb.2008.04.048
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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

Nurit Eliash, Michal Harel