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PDBsum entry 2vt4
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protein ligands metals Protein-protein interface(s) links
Receptor PDB id
2vt4

 

 

 

 

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Contents
Protein chains
274 a.a. *
Ligands
P32 ×4
SOG ×12
D10 ×2
Metals
_NA ×4
Waters ×31
* Residue conservation analysis
PDB id:
2vt4
Name: Receptor
Title: Turkey beta1 adrenergic receptor with stabilising mutations and bound cyanopindolol
Structure: Beta1 adrenergic receptor. Chain: a, b, c, d. Fragment: residues 33-243,272-276,279-367. Synonym: beta-1 adrenoceptor, beta-1 adrenoreceptor, beta-t. Engineered: yes. Mutation: yes
Source: Meleagris gallopavo. Common turkey. Organism_taxid: 9103. Cell: erythrocyte. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five.
Resolution:
2.70Å     R-factor:   0.215     R-free:   0.268
Authors: A.Warne,M.J.Serrano-Vega,J.G.Baker,R.Moukhametzianov,P.C.Edwards, R.Henderson,A.G.W.Leslie,C.G.Tate,G.F.X.Schertler
Key ref: T.Warne et al. (2008). Structure of a beta1-adrenergic G-protein-coupled receptor. Nature, 454, 486-491. PubMed id: 18594507
Date:
09-May-08     Release date:   24-Jun-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P07700  (ADRB1_MELGA) -  Beta-1 adrenergic receptor from Meleagris gallopavo
Seq:
Struc: 		483 a.a.
274 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 

 
Nature 454:486-491 (2008)
PubMed id: 18594507  
 
 
Structure of a beta1-adrenergic G-protein-coupled receptor.
T.Warne, M.J.Serrano-Vega, J.G.Baker, R.Moukhametzianov, P.C.Edwards, R.Henderson, A.G.Leslie, C.G.Tate, G.F.Schertler.
 
  ABSTRACT  
 
G-protein-coupled receptors have a major role in transmembrane signalling in most eukaryotes and many are important drug targets. Here we report the 2.7 A resolution crystal structure of a beta(1)-adrenergic receptor in complex with the high-affinity antagonist cyanopindolol. The modified turkey (Meleagris gallopavo) receptor was selected to be in its antagonist conformation and its thermostability improved by earlier limited mutagenesis. The ligand-binding pocket comprises 15 side chains from amino acid residues in 4 transmembrane alpha-helices and extracellular loop 2. This loop defines the entrance of the ligand-binding pocket and is stabilized by two disulphide bonds and a sodium ion. Binding of cyanopindolol to the beta(1)-adrenergic receptor and binding of carazolol to the beta(2)-adrenergic receptor involve similar interactions. A short well-defined helix in cytoplasmic loop 2, not observed in either rhodopsin or the beta(2)-adrenergic receptor, directly interacts by means of a tyrosine with the highly conserved DRY motif at the end of helix 3 that is essential for receptor activation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23407534 A.J.Venkatakrishnan, X.Deupi, G.Lebon, C.G.Tate, G.F.Schertler, and M.M.Babu (2013).
Molecular signatures of G-protein-coupled receptors.
  Nature, 494, 185-194.  
23051750 F.Hausch, and F.Holsboer (2012).
Structural biology: Snapshot of an activated peptide receptor.
  Nature, 490, 492-493.  
22437504 H.Wu, D.Wacker, M.Mileni, V.Katritch, G.W.Han, E.Vardy, W.Liu, A.A.Thompson, X.P.Huang, F.I.Carroll, S.W.Mascarella, R.B.Westkaemper, P.D.Mosier, B.L.Roth, V.Cherezov, and R.C.Stevens (2012).
Structure of the human κ-opioid receptor in complex with JDTic.
  Nature, 485, 327-332.
PDB code: 4djh
23051748 J.F.White, N.Noinaj, Y.Shibata, J.Love, B.Kloss, F.Xu, J.Gvozdenovic-Jeremic, P.Shah, J.Shiloach, C.G.Tate, and R.Grisshammer (2012).
Structure of the agonist-bound neurotensin receptor.
  Nature, 490, 508-513.
PDB code: 4grv
22278061 K.Haga, A.C.Kruse, H.Asada, T.Yurugi-Kobayashi, M.Shiroishi, C.Zhang, W.I.Weis, T.Okada, B.K.Kobilka, T.Haga, and T.Kobayashi (2012).
Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist.
  Nature, 482, 547-551.
PDB code: 3uon
23237917 R.C.Stevens, V.Cherezov, V.Katritch, R.Abagyan, P.Kuhn, H.Rosen, and K.Wüthrich (2012).
The GPCR Network: a large-scale collaboration to determine human GPCR structure and function.
  Nat Rev Drug Discov, 12, 25-34.  
22596164 S.Granier, A.Manglik, A.C.Kruse, T.S.Kobilka, F.S.Thian, W.I.Weis, and B.K.Kobilka (2012).
Structure of the δ-opioid receptor bound to naltrindole.
  Nature, 485, 400-404.
PDB code: 4ej4
22286059 T.Hino, T.Arakawa, H.Iwanari, T.Yurugi-Kobayashi, C.Ikeda-Suno, Y.Nakada-Nakura, O.Kusano-Arai, S.Weyand, T.Shimamura, N.Nomura, A.D.Cameron, T.Kobayashi, T.Hamakubo, S.Iwata, and T.Murata (2012).
G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody.
  Nature, 482, 237-240.
PDB codes: 3vg9 3vga
21543849 F.Gorrec, C.M.Palmer, G.Lebon, and T.Warne (2011).
Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening.
  Acta Crystallogr D Biol Crystallogr, 67, 463-470.  
21593763 G.Lebon, T.Warne, P.C.Edwards, K.Bennett, C.J.Langmead, A.G.Leslie, and C.G.Tate (2011).
Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation.
  Nature, 474, 521-525.
PDB codes: 2ydo 2ydv
21389983 J.Standfuss, P.C.Edwards, A.D'Antona, M.Fransen, G.Xie, D.D.Oprian, and G.F.Schertler (2011).
The structural basis of agonist-induced activation in constitutively active rhodopsin.
  Nature, 471, 656-660.
PDB code: 2x72
21772288 S.G.Rasmussen, B.T.DeVree, Y.Zou, A.C.Kruse, K.Y.Chung, T.S.Kobilka, F.S.Thian, P.S.Chae, E.Pardon, D.Calinski, J.M.Mathiesen, S.T.Shah, J.A.Lyons, M.Caffrey, S.H.Gellman, J.Steyaert, G.Skiniotis, W.I.Weis, R.K.Sunahara, and B.K.Kobilka (2011).
Crystal structure of the β2 adrenergic receptor-Gs protein complex.
  Nature, 477, 549-555.
PDB code: 3sn6
21228869 S.G.Rasmussen, H.J.Choi, J.J.Fung, E.Pardon, P.Casarosa, P.S.Chae, B.T.Devree, D.M.Rosenbaum, F.S.Thian, T.S.Kobilka, A.Schnapp, I.Konetzki, R.K.Sunahara, S.H.Gellman, A.Pautsch, J.Steyaert, W.I.Weis, and B.K.Kobilka (2011).
Structure of a nanobody-stabilized active state of the β(2) adrenoceptor.
  Nature, 469, 175-180.
PDB code: 3p0g
21697825 T.Shimamura, M.Shiroishi, S.Weyand, H.Tsujimoto, G.Winter, V.Katritch, R.Abagyan, V.Cherezov, W.Liu, G.W.Han, T.Kobayashi, R.C.Stevens, and S.Iwata (2011).
Structure of the human histamine H1 receptor complex with doxepin.
  Nature, 475, 65-70.
PDB code: 3rze
21228877 T.Warne, R.Moukhametzianov, J.G.Baker, R.Nehmé, P.C.Edwards, A.G.Leslie, G.F.Schertler, and C.G.Tate (2011).
The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor.
  Nature, 469, 241-244.
PDB codes: 2y00 2y01 2y02 2y03 2y04
20054398 M.P.Bokoch, Y.Zou, S.G.Rasmussen, C.W.Liu, R.Nygaard, D.M.Rosenbaum, J.J.Fung, H.J.Choi, F.S.Thian, T.S.Kobilka, J.D.Puglisi, W.I.Weis, L.Pardo, R.S.Prosser, L.Mueller, and B.K.Kobilka (2010).
Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor.
  Nature, 463, 108-112.
PDB code: 3kj6
19458711 D.M.Rosenbaum, S.G.Rasmussen, and B.K.Kobilka (2009).
The structure and function of G-protein-coupled receptors.
  Nature, 459, 356-363.  
19458709 S.H.White (2009).
Biophysical dissection of membrane proteins.
  Nature, 459, 344-346.  
18955489 I.Assil-Kishawi, T.A.Samra, D.F.Mierke, and A.B.Abou-Samra (2008).
Residue 17 of sauvagine cross-links to the first transmembrane domain of corticotropin-releasing factor receptor 1 (CRFR1).
  J Biol Chem, 283, 35644-35651.  
18936102 M.Foucaud, E.Marco, C.Escrieut, C.Low, B.Kalindjian, and D.Fourmy (2008).
Linking non-peptide ligand binding mode to activity at the human cholecystokinin-2 receptor.
  J Biol Chem, 283, 35860-35868.  
18818650 P.Scheerer, J.H.Park, P.W.Hildebrand, Y.J.Kim, N.Krauss, H.W.Choe, K.P.Hofmann, and O.P.Ernst (2008).
Crystal structure of opsin in its G-protein-interacting conformation.
  Nature, 455, 497-502.
PDB code: 3dqb
18832607 V.P.Jaakola, M.T.Griffith, M.A.Hanson, V.Cherezov, E.Y.Chien, J.R.Lane, A.P.Ijzerman, and R.C.Stevens (2008).
The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist.
  Science, 322, 1211-1217.
PDB code: 3eml
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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