Hydrophobic Cluster Analysis of G Protein-Coupled Receptors: A Powerful tool to Derive Structural and Functional Information from 2D-Representation of Protein Sequences

1993 ◽  
Vol 13 (1-4) ◽  
pp. 179-194 ◽  
Author(s):  
Klaus-Ulrich Lentes ◽  
Eric Mathieu ◽  
Rainer Bischoff
Biochimie ◽  
1990 ◽  
Vol 72 (8) ◽  
pp. 555-574 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
B. Henrissat ◽  
C. Gaboriaud ◽  
V. Bissery ◽  
A. Morgat ◽  
...  

1988 ◽  
Vol 255 (3) ◽  
pp. 901-905 ◽  
Author(s):  
B Henrissat ◽  
Y Popineau ◽  
J C Kader

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.


PROTEOMICS ◽  
2018 ◽  
Vol 18 (21-22) ◽  
pp. 1800054 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Alexis Lamiable ◽  
Jean-Paul Mornon ◽  
Isabelle Callebaut

1995 ◽  
pp. 129-144
Author(s):  
Michel T. Semertzidis ◽  
Etienne Thoreau ◽  
Anne Tasso ◽  
Bernard Henrissat ◽  
Isabelle Callebaut ◽  
...  

2018 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Isabelle Callebaut

AbstractMotivation: Detecting protein domains sharing no similarity to known domains, as stored in domain databases, is a challenging problem, particularly for unannotated proteomes, domains emerged recently, fast diverging proteins or domains with intrinsically disordered regions.Results: We developed pyHCA and HCAtk, a python API and standalone tool gathering together improved versions of previously developed methodologies, with new functionalities. The developed tools can be either used from command line or from a python API.Availability: HCAtk and pyHCA are available at https://github.com/T-B-F/pyHCA under the CeCILL-C license.


1993 ◽  
Vol 9 (1) ◽  
pp. 37-44 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
C. Gaboriaud ◽  
A. Morgat ◽  
G. Pantel ◽  
J. P. Mornon ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document