3dy9
Crystal structure of AeD7 potassium bromide soakCrystal structure of AeD7 potassium bromide soak
Structural highlights
Function[ALL2_AEDAE] Thought to be involved in blood-feeding.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe mosquito D7 salivary proteins are encoded by a multigene family related to the arthropod odorant-binding protein (OBP) superfamily. Forms having either one or two OBP domains are found in mosquito saliva. Four single-domain and one two-domain D7 proteins from Anopheles gambiae and Aedes aegypti (AeD7), respectively, were shown to bind biogenic amines with high affinity and with a stoichiometry of one ligand per protein molecule. Sequence comparisons indicated that only the C-terminal domain of AeD7 is homologous to the single-domain proteins from A. gambiae, suggesting that the N-terminal domain may bind a different class of ligands. Here, we describe the 3D structure of AeD7 and examine the ligand-binding characteristics of the N- and C-terminal domains. Isothermal titration calorimetry and ligand complex crystal structures show that the N-terminal domain binds cysteinyl leukotrienes (cysLTs) with high affinities (50-60 nM) whereas the C-terminal domain binds biogenic amines. The lipid chain of the cysLT binds in a hydrophobic pocket of the N-terminal domain, whereas binding of norepinephrine leads to an ordering of the C-terminal portion of the C-terminal domain into an alpha-helix that, along with rotations of Arg-176 and Glu-268 side chains, acts to bury the bound ligand. Multifunctionality and mechanism of ligand binding in a mosquito antiinflammatory protein.,Calvo E, Mans BJ, Ribeiro JM, Andersen JF Proc Natl Acad Sci U S A. 2009 Mar 10;106(10):3728-33. Epub 2009 Feb 20. PMID:19234127[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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