Article

You have full text access to this OnlineOpen article

The importance of valine 114 in ligand binding in β2-adrenergic receptor

  1. Makoto Arakawa1,†,
  2. Naveena Yanamala2,
  3. Jasbir Upadhyaya1,
  4. Andrew Halayko3,
  5. Judith Klein-Seetharaman2,
  6. Prashen Chelikani1,*

Article first published online: 13 NOV 2009

DOI: 10.1002/pro.285

Issue

Protein Science

Protein Science

Volume 19, Issue 1, pages 85–93, January 2010

Additional Information

How to Cite

Arakawa, M., Yanamala, N., Upadhyaya, J., Halayko, A., Klein-Seetharaman, J. and Chelikani, P. (2010), The importance of valine 114 in ligand binding in β2-adrenergic receptor. Protein Science, 19: 85–93. doi: 10.1002/pro.285

Author Information

  1. 1

    Department of Oral Biology, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0W4

  2. 2

    Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260

  3. 3

    Department of Physiology, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0W4

  1. †

    Department of Dental Sciences for Health Promotion, Hiroshima University, Hiroshima 734-8553, Japan

*Department of Oral Biology, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0W4

Publication History

  1. Issue published online: 6 JAN 2010
  2. Article first published online: 13 NOV 2009
  3. Accepted manuscript online: 13 NOV 2009 12:00AM EST
  4. Manuscript Accepted: 2 NOV 2009
  5. Manuscript Revised: 30 OCT 2009
  6. Manuscript Received: 13 AUG 2009

Funded by

  • Manitoba Medical Service Foundation (MMSF)
  • Canadian Institute of Health Research. Grant Number: ROP 92389
  • Manitoba Health Research Council (MHRC)
  • National Institutes of Health. Grant Number: NIH-NLM 2RO1LM007994-05
  • National Science Foundation. Grant Number: CAREER NSF-CC0449117
  • New Investigator Personnel Award from the Heart and Stroke Foundation of Canada (HSFC)

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article with Supporting Information (HTML) Get PDF (628K)

References

  • 1
    Lefkowitz RJ ( 2007) Seven transmembrane receptors: a brief personal retrospective. Biochim Biophys Acta 1768: 748–755.
  • 2
    Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, Kobilka BK ( 2007) GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 318: 1266–1273.
  • 3
    Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, Leslie AG, Tate CG, Schertler GF ( 2008) Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 454: 486–491.
  • 4
    Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY, Lane JR, Ijzerman AP, Stevens RC ( 2008) The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322: 1211–1217.
  • 5
    Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe HW, Hofmann KP, Ernst OP ( 2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455: 497–502.
  • 6
    Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK ( 2007) Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450: 383–387.
  • 7
    Ballesteros JA, Weinstein H. ( 1995) Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G-protein coupled receptors. Methods Neurosci 25: 366–428.
  • 8
    Ahuja S, Crocker E, Eilers M, Hornak V, Hirshfeld A, Ziliox M, Syrett N, Reeves PJ, Khorana HG, Sheves M, Smith SO ( 2009) Location of the retinal chromophore in the activated state of rhodopsin*. J Biol Chem 284: 10190–10201.
  • 9
    Ahuja S, Hornak V, Yan EC, Syrett N, Goncalves JA, Hirshfeld A, Ziliox M, Sakmar TP, Sheves M, Reeves PJ, Smith SO, Eilers M ( 2009) Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation. Nat Struct Mol Biol 16: 168–175.
  • 10
    Strader CD, Sigal IS, Register RB, Candelore MR, Rands E, Dixon RAF ( 1987) Identification of residues required for ligand binding to the β-adrenergic receptor. Proc Natl Acad Sci USA 84: 4384–4388.
  • 11
    Strader CD, Sigal IS, Candelore MR, Rands E, Hill WS, Dixon RA ( 1988) Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function. J Biol Chem 263: 10267–10271.
  • 12
    Chelikani P, Hornak V, Eilers M, Reeves PJ, Smith SO, RajBhandary UL, Khorana HG ( 2007) Role of group-conserved residues in the helical core of beta2-adrenergic receptor. Proc Natl Acad Sci USA 104: 7027–7032.
  • 13
    Noda K, Saad Y, Graham RM, Karnik SS ( 1994) The high affinity state of the beta 2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines. J Biol Chem 269: 6743–6752.
  • 14
    Kim JM, Hwa J, Garriga P, Reeves PJ, RajBhandary UL, Khorana HG ( 2005) Light-driven activation of beta 2-adrenergic receptor signaling by a chimeric rhodopsin containing the beta 2-adrenergic receptor cytoplasmic loops. Biochemistry 44: 2284–2292.
  • 15
    DeLano WL ( 2002) The PyMOL Molecular Graphics System. DeLano Scientific, Palo Alto, CA.
  • 16
    Goodsell DS, Morris GM, Olson AJ ( 1996) Automated docking of flexible ligands: applications of AutoDock. J Mol Recognit 9: 1–5.
    Direct Link:
  • 17
    Morris GM, Huey R, Olson AJ ( 2008) Using AutoDock for ligand-receptor docking. Curr Protoc Bioinformatics Chapter 8:Unit 8 14.
  • 18
    Abagyan RA, Raush E, Budagyan L, Totrov M ( 2007) ICM Browser Pro. Version 3.6. La Jolla, CA: MolSoft LLC.
  • 19
    Katritch V, Reynolds KA, Cherezov V, Hanson MA, Roth CB, Yeager M, Abagyan R ( 2009) Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes. J Mol Recognit 22: 307–318.
    Direct Link:
  • 20
    Vanni S, Neri M, Tavernelli I, Rothlisberger U ( 2009) Observation of “ionic lock” formation in molecular dynamics simulations of wild-type beta(1) and beta(2) adrenergic receptors. Biochemistry 48: 4789–4797.
  • 21
    Oprian DD, Molday RS, Kaufman RJ, Khorana HG ( 1987) Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proc Natl Acad Sci USA 84: 8874–8878.
  • 22
    Chelikani P, Reeves PJ, Rajbhandary UL, Khorana HG ( 2006) The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line. Protein Sci 15: 1433–1440.
    Direct Link:
  • 23
    Eswar N, Webb B, Marti-Renom MA, Madhusudhan MS, Eramian D, Shen MY, Pieper U, Sali A ( 2007) Comparative protein structure modeling using MODELLER. Curr Protoc Protein Sci Chapter 2:Unit 2.9.
  • 24
    Yanamala N, Tirupula KC, Klein-Seetharaman J ( 2008) Preferential binding of allosteric modulators to active and inactive conformational states of metabotropic glutamate receptors. BMC Bioinformatics 9: S16.
  • 25
    Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947–2948.
  • 26
    Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB, III, Snoeyink J, Richardson JS, Richardson DC ( 2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375–W383.
View Full Article with Supporting Information (HTML) Get PDF (628K)