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<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd> <responseDate>2018-01-15T15:42:31Z</responseDate> <request identifier=oai:HAL:inserm-00366309v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:inserm-00366309v1</identifier> <datestamp>2017-12-21</datestamp> <setSpec>type:ART</setSpec> <setSpec>subject:sdv</setSpec> <setSpec>subject:info</setSpec> <setSpec>collection:SANTE_PUB_INSERM</setSpec> <setSpec>collection:INSERM</setSpec> <setSpec>collection:UNIV-PARIS7</setSpec> <setSpec>collection:UNIV-REUNION</setSpec> <setSpec>collection:USPC</setSpec> <setSpec>collection:UNIV-AG</setSpec> </header> <metadata><dc> <publisher>HAL CCSD</publisher> <title lang=it>In Silico Studies on DARC.</title> <creator>De Brevern, Alexandre</creator> <creator>Autin, Ludovic</creator> <creator>Colin, Yves</creator> <creator>Bertrand, Olivier</creator> <creator>Etchebest, Catherine</creator> <contributor>Protéines de la membrane érythrocytaire et homologues non-érythroides ; Université des Antilles et de la Guyane (UAG) - Institut National de la Transfusion Sanguine [Paris] (INTS) - Université Paris Diderot - Paris 7 (UPD7) - Université de la Réunion (UR) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor> <contributor>- Région Ile-De-France - Polonium grant 14287VM “Refinement of the studies on specificity of monoclonal antibody 2C3 directed against Duffy/DARC protein”.</contributor> <description>International audience</description> <source>Infectious disorders drug targets</source> <identifier>inserm-00366309</identifier> <identifier>http://www.hal.inserm.fr/inserm-00366309</identifier> <identifier>http://www.hal.inserm.fr/inserm-00366309/document</identifier> <identifier>http://www.hal.inserm.fr/inserm-00366309/file/de_Brevern_Autin_Bertrand_Colin_Etchebest.pdf</identifier> <identifier>http://www.hal.inserm.fr/inserm-00366309/file/inserm-00366309_edited.pdf</identifier> <source>http://www.hal.inserm.fr/inserm-00366309</source> <source>Infectious disorders drug targets, 2009, 9 (3), pp.289-303</source> <identifier>PUBMED : 19519483</identifier> <relation>info:eu-repo/semantics/altIdentifier/pmid/19519483</relation> <language>en</language> <subject lang=en>Plasmodium vivax</subject> <subject lang=en>Duffy Antigen</subject> <subject lang=en>Receptor for Chemokine</subject> <subject lang=en>CXCL-8</subject> <subject lang=en>Duffy Binding Protein</subject> <subject lang=en>chemokines</subject> <subject lang=en>malaria</subject> <subject lang=en>Plasmodium vivax.</subject> <subject>[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology</subject> <subject>[SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]</subject> <subject>[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]</subject> <subject>[SDV.IMM] Life Sciences [q-bio]/Immunology</subject> <subject>[SDV.SPEE] Life Sciences [q-bio]/Santé publique et épidémiologie</subject> <type>info:eu-repo/semantics/article</type> <type>Journal articles</type> <description lang=en>The Duffy Antigen/Receptor for Chemokine (DARC) is a seven segment transmembrane protein. It was firstly discovered as a blood group antigen and was the first specific gene locus assigned to a specific autosome in man. It became more famous as an erythrocyte receptor for malaria parasites (Plasmodium vivax and Plasmodium knowlesi), and finally for chemokines. DARC is an unorthodox chemokine receptor as (i) it binds chemokines of both CC and CXC classes and (ii) it lacks the Asp-Arg-Tyr consensus motif in its second cytoplasmic loop hence cannot couple to G proteins and activate their signaling pathways. DARC had also been associated to cancer progression, numerous inflammatory diseases, and possibly to AIDS. In this review, we will summarize important biological data on DARC. Then we shall focus on recent development of the elaboration and analyzes of structural models of DARC. We underline the difficulty to propose pertinent structural models of transmembrane protein using comparative modeling process, and other dedicated approaches as the Protein Blocks. The chosen structural models encompass most of the biochemical data known to date. Finally, we present recent development of protein - protein docking between DARC structural models and CXCL-8 structures. We propose a hierarchal search based on separated rigid and flexible docking.</description> <date>2009-06</date> <rights>info:eu-repo/semantics/OpenAccess</rights> </dc> </metadata> </record> </GetRecord> </OAI-PMH>