Structure and function of A41, a vaccinia virus chemokine binding protein

• Main Authors: Bahar M.W., Kenyon J.C., Putz M.M., Abrescia N.G.A., Pease J.E., Wise E.L., Stuart D.I., Smith G.L., Grimes J.M.
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: 2019
• Subjects: beta chemokine; binding protein; chemokine CCL25; chemokine CCL28; chemokine inhibitor; chemokine inhibitor vCCI; eotaxin 3; glycosaminoglycan; heparin; protein vCKBP; secondary lymphoid tissue chemokine; unclassified drug; virus protein A41; virus protein; A41L gene; animal cell; article; binding site; CD8+ T lymphocyte; concentration response; controlled study; crystal structure; dose response; drug mechanism; human; immune response; ligand binding; nonhuman; optical resolution; protein protein interaction; protein secretion; protein structure; sequence homology; structure activity relation; surface plasmon resonance; Vaccinia virus; virus gene; virus replication; amino acid sequence; animal; biological model; chemistry; chemotaxis; crystallization; cytology; immunology; leukocyte; metabolism; molecular genetics; mouse; physiology; protein binding; protein conformation; Murinae; Poxviridae; Amino Acid Sequence; Animals; CD8-Positive T-Lymphocytes; Chemokines, CC; Chemotaxis; Crystallization; Glycosaminoglycans; Heparin; Humans; Leukocytes; Mice; Models, Biological; Molecular Sequence Data; Protein Binding; Protein Conformation; Structure-Activity Relationship; Viral Proteins
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161860
• Institution: National University of Singapore

10.1371/journal.ppat.0040005