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 Abstract"AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-agglutinin, a cell surface glycoprotein involved in cell-cell interactions during mating"    Next AbstractDual action of phosphonate herbicides in plants affected by herbivore--model study on black bean aphid Aphis fabae rearing on broad bean Vicia faba plants »

Protein Sci


Title:Homology modeling of an immunoglobulin-like domain in the Saccharomyces cerevisiae adhesion protein alpha-agglutinin
Author(s):Lipke PN; Chen MH; de Nobel H; Kurjan J; Kahn PC;
Address:"Department of Biological Sciences, Hunter College of the City University of New York, New York 10021, USA"
Journal Title:Protein Sci
Year:1995
Volume:4
Issue:10
Page Number:2168 - 2178
DOI: 10.1002/pro.5560041023
ISSN/ISBN:0961-8368 (Print) 1469-896X (Electronic) 0961-8368 (Linking)
Abstract:"The Saccharomyces cerevisiae adhesion protein alpha-agglutinin is expressed by cells of alpha mating type. On the basis of sequence similarities, alpha-agglutinin has been proposed to contain variable-type immunoglobulin-like (IgV) domains. The low level of sequence similarity to IgV domains of known structure made homology modeling using standard sequence-based alignment algorithms impossible. We have therefore developed a secondary structure-based method that allowed homology modeling of alpha-aggulutinin domain III, the domain most similar to IgV domains. The model was assessed and where necessary refined to accommodate information obtained by biochemical and molecular genetic approaches, including the positions of a disulfide bond, glycosylation sites, and proteolytic sites. The model successfully predicted surface exposure of glycosylation and proteolytic sites, as well as identifying residues essential for binding activity. One side of the domain was predicted to be covered by carbohydrate residues. Surface accessibility and volume packing analyses showed that the regions of the model that have greatest sequence dissimilarity from the IgV consensus sequence are poorly structured in the biophysical sense. Nonetheless, the utility of the model suggests that these alignment and testing techniques should be of general use for building and testing of models of proteins that share limited sequence similarity with known structures"
Keywords:"Agglutinins/chemistry Amino Acid Sequence Consensus Sequence Immunoglobulin Variable Region/*chemistry Mating Factor Models, Molecular Molecular Sequence Data Peptide Biosynthesis Peptides/*chemistry *Protein Conformation *Protein Structure, Secondary Sac;"
Notes:"MedlineLipke, P N Chen, M H de Nobel, H Kurjan, J Kahn, P C eng Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1995/10/01 Protein Sci. 1995 Oct; 4(10):2168-78. doi: 10.1002/pro.5560041023"

 
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 26-12-2024