Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Callebaut, I.
Right arrow Articles by Mornon, J. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Callebaut, I.
Right arrow Articles by Mornon, J. P.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 9, Issue 7 1382-1390, Copyright © 2000 by The Protein Society


HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold [In Process Citation]

I Callebaut, D Gilges, I Vigon and JP Mornon
Systemes Moleculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universite Paris 6, France. callebau@lmcp.jussieu.fr

Domains belonging to the immunoglobulin-like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of domains, the HYR family, which is predicted to belong to this fold, and which appears to be involved in cellular adhesion. HYR domains were identified in several eukaryotic proteins, often associated with Complement Control Protein (CCP) modules or arranged in multiple copies. Our analysis provides a sequence and structural basis for understanding the role of these domains in interaction mechanisms and leads to further characterization of heretofore undescribed repeated domains with similar folds found in several bacterial proteins involved in enzymatic activities (some chitinases) or in cell surface adhesion (streptococcal C-alpha antigen).
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
G. Manning, S. L. Young, W. T. Miller, and Y. Zhai
From the Cover: The protist, Monosiga brevicollis, has a tyrosine kinase signaling network more elaborate and diverse than found in any known metazoan
PNAS, July 15, 2008; 105(28): 9674 - 9679.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
T. W. Loehfelm, N. R. Luke, and A. A. Campagnari
Identification and Characterization of an Acinetobacter baumannii Biofilm-Associated Protein
J. Bacteriol., February 1, 2008; 190(3): 1036 - 1044.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
H. Bierne and P. Cossart
Listeria monocytogenes Surface Proteins: from Genome Predictions to Function
Microbiol. Mol. Biol. Rev., June 1, 2007; 71(2): 377 - 397.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
P. Roll, G. Rudolf, S. Pereira, B. Royer, I. E. Scheffer, A. Massacrier, M.-P. Valenti, N. Roeckel-Trevisiol, S. Jamali, C. Beclin, et al.
SRPX2 mutations in disorders of language cortex and cognition
Hum. Mol. Genet., April 1, 2006; 15(7): 1195 - 1207.
[Abstract] [Full Text] [PDF]


Home page
Clin. Microbiol. Rev.Home page
G. Lindahl, M. Stalhammar-Carlemalm, and T. Areschoug
Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens
Clin. Microbiol. Rev., January 1, 2005; 18(1): 102 - 127.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. J. Arrizubieta, A. Toledo-Arana, B. Amorena, J. R. Penades, and I. Lasa
Calcium Inhibits Bap-Dependent Multicellular Behavior in Staphylococcus aureus
J. Bacteriol., November 15, 2004; 186(22): 7490 - 7498.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
N. Kamei and C. G. Glabe
The species-specific egg receptor for sea urchin sperm adhesion is EBR1,a novel ADAMTS protein
Genes & Dev., October 15, 2003; 17(20): 2502 - 2507.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
C. Cucarella, M. A. Tormo, E. Knecht, B. Amorena, I. Lasa, T. J. Foster, and J. R. Penades
Expression of the Biofilm-Associated Protein Interferes with Host Protein Receptors of Staphylococcus aureus and Alters the Infective Process
Infect. Immun., June 1, 2002; 70(6): 3180 - 3186.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.