Hostname: page-component-78c5997874-s2hrs Total loading time: 0 Render date: 2024-11-15T23:24:31.922Z Has data issue: false hasContentIssue false

HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold

Published online by Cambridge University Press:  01 July 2000

ISABELLE CALLEBAUT
Affiliation:
Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, Paris, France
DELPHINE GILGÈS
Affiliation:
INSERM U474, Hôpital Henri Mondor, Créteil, France
ISABELLE VIGON
Affiliation:
INSERM U474, Hôpital Henri Mondor, Créteil, France
JEAN-PAUL MORNON
Affiliation:
Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, Paris, France
Get access

Abstract

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).

Type
FOR THE RECORD
Copyright
2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)