dc.contributor.author | Chao, Ta-Hsiang | |
dc.contributor.author | Ember, Julia A. | |
dc.contributor.author | Wang, Meiying | |
dc.contributor.author | Bayón Prieto, Yolanda | |
dc.contributor.author | Hugli, Tony E. | |
dc.contributor.author | Ye, Richard D. | |
dc.date.accessioned | 2021-07-19T06:09:55Z | |
dc.date.available | 2021-07-19T06:09:55Z | |
dc.date.issued | 1999 | |
dc.identifier.citation | Journal of Biological Chemistry, 1999, vol. 274, n. 14, p. 9721-9728 | es |
dc.identifier.issn | 0021-9258 | es |
dc.identifier.uri | https://uvadoc.uva.es/handle/10324/47501 | |
dc.description | Producción Científica | es |
dc.description.abstract | The C3a anaphylatoxin receptor (C3aR) is a G protein-coupled receptor with an unusually large second extra-cellular loop (e2 loop,;172 amino acids). To determinethe function of this unique structure, chimeric and de-letion mutants were prepared and analyzed in trans-fected RBL-2H3 cells. Whereas replacement of the C3aRN-terminal segment with that from the human C5a re-ceptor had minimal effect on C3a binding, substitutionof the e2 loop with a smaller e2 loop from the C5a recep-tor (C5aR) abolished binding of125I-C3a and C3a-stimu-lated calcium mobilization. However, as much as 65% ofthe e2 loop sequence (amino acids 198 –308) may be re-moved without affecting C3a binding or calcium re-sponses. The e2 loop sequences adjacent to the trans-membrane domains contain multiple aspartate residuesand are found to play an important role in C3a bindingbased on deletion mutagenesis. Replacement of five as-partate residues in the e2 loop with lysyl residues sig-nificantly compromised both the binding and functionalcapabilities of the C3a receptor mediated by intact C3aor by two C3a analog peptides. These data suggest atwo-site C3a-C3aR interaction model similar to that es-tablished for C5a/C5aR. The anionic residues near the Nand C termini of the C3aR e2 loop constitute a non-effector secondary interaction site with cationic resi-dues in the C-terminal helical region of C3a, whereas theC3a C-terminal sequence LGLAR engages the primaryeffector site in C3aR. | es |
dc.format.mimetype | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Elsevier | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject.classification | Calcio | es |
dc.subject.classification | Receptor C3a humano | es |
dc.subject.classification | Human C3a receptorin | es |
dc.title | Role of the second extracellular loop of human C3a receptor in agonist binding and receptor function | es |
dc.type | info:eu-repo/semantics/article | es |
dc.rights.holder | © Elsevier | es |
dc.identifier.doi | 10.1074/jbc.274.14.9721 | es |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S002192581987309X | es |
dc.identifier.publicationfirstpage | 9721 | es |
dc.identifier.publicationissue | 14 | es |
dc.identifier.publicationlastpage | 9728 | es |
dc.identifier.publicationtitle | Journal of Biological Chemistry | es |
dc.identifier.publicationvolume | 274 | es |
dc.peerreviewed | SI | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.type.hasVersion | info:eu-repo/semantics/publishedVersion | es |
dc.subject.unesco | 24 Ciencias de la Vida | es |