HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold
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 identi...
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| Published in | Protein science Vol. 9; no. 7; pp. 1382 - 1390 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Bristol
Cambridge University Press
01.07.2000
Cold Spring Harbor Laboratory Press Wiley |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0961-8368 1469-896X |
| DOI | 10.1110/ps.9.7.1382 |
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| 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). |
|---|---|
| AbstractList | 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).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). 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). 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). |
| Author | GILGÈS, DELPHINE VIGON, ISABELLE CALLEBAUT, ISABELLE MORNON, JEAN-PAUL |
| AuthorAffiliation | Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Université Paris 6, France |
| AuthorAffiliation_xml | – name: Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Université Paris 6, France |
| Author_xml | – sequence: 1 givenname: ISABELLE surname: CALLEBAUT fullname: CALLEBAUT, ISABELLE organization: Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, Paris, France – sequence: 2 givenname: DELPHINE surname: GILGÈS fullname: GILGÈS, DELPHINE organization: INSERM U474, Hôpital Henri Mondor, Créteil, France – sequence: 3 givenname: ISABELLE surname: VIGON fullname: VIGON, ISABELLE organization: INSERM U474, Hôpital Henri Mondor, Créteil, France – sequence: 4 givenname: JEAN-PAUL surname: MORNON fullname: MORNON, JEAN-PAUL organization: Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, Paris, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10933504$$D View this record in MEDLINE/PubMed https://hal.science/hal-02401000$$DView record in HAL |
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| Copyright | 2000 The Protein Society Copyright © 2000 The Protein Society Distributed under a Creative Commons Attribution 4.0 International License |
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| Keywords | fibronectin type III polycystic kidney disease adhesion iterative database search complement control protein hydrophobic cluster analysis hyalin |
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| Snippet | 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 belonging to the immunoglobulin‐like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of... Domains belonging to the immunoglobulin-like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of... |
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| SubjectTerms | adhesion Amino Acid Sequence Bacterial Proteins - chemistry Biochemistry, Molecular Biology Cell Adhesion - physiology complement control protein Extracellular Matrix Proteins - chemistry Extracellular Matrix Proteins - metabolism fibronectin type III Fibronectins - chemistry FOR THE RECORD hyalin Hyalin - chemistry hydrophobic cluster analysis Immunoglobulins - chemistry iterative database search Life Sciences Molecular Sequence Data polycystic kidney disease Protein Folding Proteins - chemistry Repetitive Sequences, Amino Acid Sequence Homology, Amino Acid Structural Biology TRPP Cation Channels |
| Title | HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold |
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