Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractAplysia seductin is a water-borne protein pheromone that acts in concert with attractin to stimulate mate attraction    Next AbstractNewly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia »

Peptides


Title:"Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness"
Author(s):Cummins SF; Schein CH; Xu Y; Braun W; Nagle GT;
Address:"Department of Neuroscience and Cell Biology, Medical Research Building, Room 2.138, University of Texas Medical Branch, Galveston, TX 77555-1069, USA"
Journal Title:Peptides
Year:2005
Volume:26
Issue:1
Page Number:121 - 129
DOI: 10.1016/j.peptides.2004.07.017
ISSN/ISBN:0196-9781 (Print) 0196-9781 (Linking)
Abstract:"The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel alpha-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific"
Keywords:"Amino Acid Sequence Animals Aplysia/anatomy & histology/*metabolism Glycoproteins/chemistry/genetics/*metabolism Molecular Sequence Data Pheromones/chemistry/genetics/*metabolism Protein Structure, Tertiary;neuroscience;"
Notes:"MedlineCummins, Scott F Schein, Catherine H Xu, Yuan Braun, Werner Nagle, Gregg T eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review 2005/01/01 Peptides. 2005 Jan; 26(1):121-9. doi: 10.1016/j.peptides.2004.07.017"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 25-11-2024