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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>2018-01-15T15:43:33Z</responseDate> <request identifier=oai:HAL:inserm-00143373v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:inserm-00143373v1</identifier> <datestamp>2017-12-21</datestamp> <setSpec>type:ART</setSpec> <setSpec>subject:sdv</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=en>A structural model of a seven-transmembrane helix receptor: the Duffy antigen/receptor for chemokine (DARC).</title> <creator>De Brevern, Alexandre</creator> <creator>Wong, H.</creator> <creator>Tournamille, Christophe</creator> <creator>Colin, Yves</creator> <creator>Le Van Kim, Caroline</creator> <creator>Etchebest, Catherine</creator> <contributor>Bioinformatique génomique et moléculaire ; Université Paris Diderot - Paris 7 (UPD7) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor> <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>This work was supported by grants from the French Institute for Health and Medical Research (INSERM), University Paris 7-Denis-Diderot, the Ministère de la Recherche and from “Action Bioinformatique inter EPST” number 4B005F and 2003–2004 (“Outil informatique intégré en Génomique Structurale. Vers une prédiction de la structure tridimensionnelle d'une protéine à partir de sa séquence.”).</contributor> <source>ISSN: 0006-3002</source> <source>BBA - Biochimica et Biophysica Acta</source> <publisher>Elsevier</publisher> <identifier>inserm-00143373</identifier> <identifier>http://www.hal.inserm.fr/inserm-00143373</identifier> <identifier>http://www.hal.inserm.fr/inserm-00143373/document</identifier> <identifier>http://www.hal.inserm.fr/inserm-00143373/file/de_Brevern_BBA_2005.pdf</identifier> <source>http://www.hal.inserm.fr/inserm-00143373</source> <source>BBA - Biochimica et Biophysica Acta, Elsevier, 2005, 1724 (3), pp.288-306. 〈10.1016/j.bbagen.2005.05.016〉</source> <identifier>DOI : 10.1016/j.bbagen.2005.05.016</identifier> <relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2005.05.016</relation> <identifier>PUBMED : 16046070</identifier> <relation>info:eu-repo/semantics/altIdentifier/pmid/16046070</relation> <language>en</language> <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>[SDV.IMM] Life Sciences [q-bio]/Immunology</subject> <subject>[SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases</subject> <subject>[SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology</subject> <type>info:eu-repo/semantics/article</type> <type>Journal articles</type> <description lang=en>The Duffy antigen/receptor for chemokine (DARC) is an erythrocyte receptor for malaria parasites (Plasmodium vivax and Plasmodium knowlesi) and for chemokines. In contrast to other chemokine receptors, DARC is a promiscuous receptor that binds chemokines of both CC and CXC classes. The four extracellular domains (ECDs) of DARC are essential for its interaction with chemokines, whilst the first (ECD1) is sufficient for the interaction with malaria erythrocyte-binding protein. In this study, we elaborate and analyze structural models of the DARC. The construction of the 3D models is based on a comparative modeling process and on the use of many procedures to predict transmembrane segments and to detect far homologous proteins with known structures. Threading, ab initio, secondary structure and Protein Blocks approaches are used to build a very large number of models. The conformational exploration of the ECDs is performed with simulated annealing. The second and fourth ECDs are strongly constrained. On the contrary, the ECD1 is highly flexible, but seems composed of three consecutive regions: a small beta-sheet, a linker region and a structured loop. The chosen structural models encompass most of the biochemical features and reflect the known experimental data. They may be used to analyze functional interaction properties.</description> <date>2005-08-05</date> </dc> </metadata> </record> </GetRecord> </OAI-PMH>