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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| Veröffentlicht in: | Protein science 2000-07, Vol.9 (7), p.1382-1390 |
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| creator | CALLEBAUT, ISABELLE GILGÈS, DELPHINE VIGON, ISABELLE MORNON, JEAN-PAUL |
| description | 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). |
| doi_str_mv | 10.1110/ps.9.7.1382 |
| format | Article |
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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).</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.9.7.1382</identifier><identifier>PMID: 10933504</identifier><language>eng</language><publisher>Bristol: Cambridge University Press</publisher><subject>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</subject><ispartof>Protein science, 2000-07, Vol.9 (7), p.1382-1390</ispartof><rights>2000 The Protein Society</rights><rights>Copyright © 2000 The Protein Society</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5592-e57bdc5ea4db6a9f1fd6cb0d355d70e6d481118c5c109fe77f8a155d259647233</citedby><cites>FETCH-LOGICAL-c5592-e57bdc5ea4db6a9f1fd6cb0d355d70e6d481118c5c109fe77f8a155d259647233</cites><orcidid>0000-0003-3124-887X ; 0000-0002-9552-8902</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144677/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144677/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10933504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02401000$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>CALLEBAUT, ISABELLE</creatorcontrib><creatorcontrib>GILGÈS, DELPHINE</creatorcontrib><creatorcontrib>VIGON, ISABELLE</creatorcontrib><creatorcontrib>MORNON, JEAN-PAUL</creatorcontrib><title>HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>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).</description><subject>adhesion</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cell Adhesion - physiology</subject><subject>complement control protein</subject><subject>Extracellular Matrix Proteins - chemistry</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>fibronectin type III</subject><subject>Fibronectins - chemistry</subject><subject>FOR THE RECORD</subject><subject>hyalin</subject><subject>Hyalin - chemistry</subject><subject>hydrophobic cluster analysis</subject><subject>Immunoglobulins - chemistry</subject><subject>iterative database search</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>polycystic kidney disease</subject><subject>Protein Folding</subject><subject>Proteins - chemistry</subject><subject>Repetitive Sequences, Amino Acid</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structural Biology</subject><subject>TRPP Cation Channels</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFrFDEUxoModls9eZc5CdLOmkySyeQilKJuYaFSFPQUMpM3u6mZyTaZWe1_b4ZZSi3FU0Le73153_sQekPwkhCCP-ziUi7FktCqeIYWhJUyr2T54zlaYFmSvKJldYSOY7zBGDNS0JfoiGBJKcdsgdrVz-uzTPcZ_BmCbsC50emQdd6MDjLb773bg0mX7L6mzRai9X3qMlkAp4cEDD4btqmh68beb5yvR2f73NlfkLXemVfoRatdhNeH8wR9__zp28UqX199ubw4X-cN57LIgYvaNBw0M3WpZUtaUzY1NpRzIzCUhlXJctXwJjloQYi20iTVCi5LJgpKT9DHWXc31h2YBvrkyqldsJ0Od8prq_6t9HarNn6vCsJYKUQSeD8LbB-1rc7XanrDBcMkbXJPEvvu8FnwtyPEQXU2TmvSPfgxKkEEZVxOU53OYBN8jAHae2WC1ZSh2kUllVBThol--9DDA3YOLQF0Bn5bB3f_01Jfr68kFgfZ_DCE7upgzQbUjR9Dn-J4coy_Esy3tQ</recordid><startdate>20000701</startdate><enddate>20000701</enddate><creator>CALLEBAUT, ISABELLE</creator><creator>GILGÈS, DELPHINE</creator><creator>VIGON, ISABELLE</creator><creator>MORNON, JEAN-PAUL</creator><general>Cambridge University Press</general><general>Cold Spring Harbor Laboratory Press</general><general>Wiley</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3124-887X</orcidid><orcidid>https://orcid.org/0000-0002-9552-8902</orcidid></search><sort><creationdate>20000701</creationdate><title>HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold</title><author>CALLEBAUT, ISABELLE ; GILGÈS, DELPHINE ; VIGON, ISABELLE ; MORNON, JEAN-PAUL</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5592-e57bdc5ea4db6a9f1fd6cb0d355d70e6d481118c5c109fe77f8a155d259647233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>adhesion</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Cell Adhesion - physiology</topic><topic>complement control protein</topic><topic>Extracellular Matrix Proteins - chemistry</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>fibronectin type III</topic><topic>Fibronectins - chemistry</topic><topic>FOR THE RECORD</topic><topic>hyalin</topic><topic>Hyalin - chemistry</topic><topic>hydrophobic cluster analysis</topic><topic>Immunoglobulins - chemistry</topic><topic>iterative database search</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>polycystic kidney disease</topic><topic>Protein Folding</topic><topic>Proteins - chemistry</topic><topic>Repetitive Sequences, Amino Acid</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structural Biology</topic><topic>TRPP Cation Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CALLEBAUT, ISABELLE</creatorcontrib><creatorcontrib>GILGÈS, DELPHINE</creatorcontrib><creatorcontrib>VIGON, ISABELLE</creatorcontrib><creatorcontrib>MORNON, JEAN-PAUL</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CALLEBAUT, ISABELLE</au><au>GILGÈS, DELPHINE</au><au>VIGON, ISABELLE</au><au>MORNON, JEAN-PAUL</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2000-07-01</date><risdate>2000</risdate><volume>9</volume><issue>7</issue><spage>1382</spage><epage>1390</epage><pages>1382-1390</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><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).</abstract><cop>Bristol</cop><pub>Cambridge University Press</pub><pmid>10933504</pmid><doi>10.1110/ps.9.7.1382</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-3124-887X</orcidid><orcidid>https://orcid.org/0000-0002-9552-8902</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Protein science, 2000-07, Vol.9 (7), p.1382-1390 |
| issn | 0961-8368 1469-896X |
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| source | MEDLINE; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 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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