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<datestamp>2018-01-11</datestamp>
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<publisher>HAL CCSD</publisher>
<title lang=en>Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures</title>
<creator>Callebaut, I.</creator>
<creator>Dulin, F.</creator>
<creator>Bertrand, O.</creator>
<creator>Ripoche, P.</creator>
<creator>Mouro, I.</creator>
<creator>Colin, Y.</creator>
<creator>Mornon, J.-P.</creator>
<creator>Cartron, J.-P.</creator>
<contributor>Institut de minéralogie et de physique des milieux condensés (IMPMC) ; Université Pierre et Marie Curie - Paris 6 (UPMC) - IPG PARIS - Université Paris Diderot - Paris 7 (UPD7) - Centre National de la Recherche Scientifique (CNRS)</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>
<description>International audience</description>
<source>ISSN: 1246-7820</source>
<source>Transfusion Clinique et Biologique</source>
<publisher>Elsevier</publisher>
<identifier>hal-00112914</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00112914</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00112914</source>
<source>Transfusion Clinique et Biologique, Elsevier, 2006, 13, pp.70-84. 〈10.1016/j.tracli.2006.02.001〉</source>
<identifier>DOI : 10.1016/j.tracli.2006.02.001</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.tracli.2006.02.001</relation>
<language>en</language>
<subject lang=fr>Hydrophobic cluster analysis</subject>
<subject lang=fr>Protein modeling</subject>
<subject lang=fr>Rh blood group</subject>
<subject lang=fr>Rh glycoproteins</subject>
<subject lang=fr>Ammonium transport</subject>
<subject lang=fr>Amt/Mep/Rh superfamily Mots clés: Amas hydrophobes</subject>
<subject lang=fr>Modélisation protéique</subject>
<subject lang=fr>Rh</subject>
<subject lang=fr>Groupes sanguins</subject>
<subject lang=fr>Glycoprotéines Rh</subject>
<subject lang=fr>Transport d'amonium</subject>
<subject lang=fr>Superfamille Amt/Mep/Rh</subject>
<subject>[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Rh (Rhesus) is a major blood group system in man, which is clinically significant in transfusion medicine. Rh antigens are carried by an oligomer of two major erythroid specific polypeptides, the Rh (D and CcEe) proteins and the RhAG glycoprotein, that shared a common predicted structure with 12 transmembrane a-helices (M0 to M11). Non erythroid homologues of these proteins have been identified (RhBG and RhCG), notably in diverse organs specialized in ammonia production and excretion, such as kidney, liver and intestine. Phylogenetic studies and experimental evidence have shown that these proteins belong to the Amt/Mep/Rh protein superfamily of ammonium/methylammonium permease, but another view suggests that Rh proteins might function as CO2 gas channels. Until recently no information on the structure of these proteins were available. However, in the last two years, new insight has been gained into the structural features of Rh proteins (through the determination of the crystal structures of bacterial AmtB and archeaebacterial Amt-1. Here, models of the subunit and oligomeric architecture of human Rh proteins are proposed, based on a refined alignment with and crystal structure of the bacterial ammonia transporter AmtB, a member of the Amt/Mep/Rh superfamily. This alignment was performed considering invariant structural features, which were revealed through Hydrophobic Cluster Analysis, and led to propose alternative predictions for the less conserved regions, particularly in the N-terminal sequences. The Rh models, on which an additional Rh-specific, N-terminal helix M0 was tentatively positioned, were further assessed through the consideration of biochemical and immunochemical data, as well as of stereochemical and topological constraints. These models highlighted some Rh specific features that have not yet been reported. Among these, are the prediction of some critical residues, which may play a role in the channel function, but also in the stability of the subunit structure and oligomeric assembly. These results provide a basis to further understand the structure/function relationships of Rh proteins, and the alterations occurring in variant phenotypes.</description>
<date>2006</date>
</dc>
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