Structure of the Tyrosine-sulfated C5a Receptor N Terminus in Complex with Chemotaxis Inhibitory Protein of Staphylococcus aureus
Open Access
- 1 May 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (18) , 12363-12372
- https://doi.org/10.1074/jbc.m808179200
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Tyrosine Sulfation Is Prevalent in Human Chemokine Receptors Important in Lung DiseaseAmerican Journal of Respiratory Cell and Molecular Biology, 2008
- Function, structure and therapeutic potential of complement C5a receptorsBritish Journal of Pharmacology, 2007
- Characterisation of receptor binding by the chemotaxis inhibitory protein of Staphylococcus aureus and the effects of the host immune responseMolecular Immunology, 2007
- CXCR3 Requires Tyrosine Sulfation for Ligand Binding and a Second Extracellular Loop Arginine Residue for Ligand-Induced ChemotaxisMolecular and Cellular Biology, 2006
- Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1α (SDF-1α/CXCL12)Journal of Molecular Biology, 2006
- The Structure of the C5a Receptor-blocking Domain of Chemotaxis Inhibitory Protein of Staphylococcus aureus is Related to a Group of Immune Evasive MoleculesJournal of Molecular Biology, 2005
- Potent Cyclic Antagonists of the Complement C5a Receptor on Human Polymorphonuclear Leukocytes. Relationships between Structures and ActivityMolecular Pharmacology, 2004
- Chemotaxis Inhibitory Protein of Staphylococcus aureus, a Bacterial Antiinflammatory AgentThe Journal of Experimental Medicine, 2004
- Sulfated Tyrosines Contribute to the Formation of the C5a Docking Site of the Human C5a Anaphylatoxin ReceptorThe Journal of Experimental Medicine, 2001
- Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance dataBiochemistry, 1989