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2vt4
From Proteopedia
| 2vt4, resolution 2.70Å () | |||||||||
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| Ligands: | , , , | ||||||||
| Related: | 1dep, 2rh1, 2r4r, 2r4s | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL
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.
Structure of a beta1-adrenergic G-protein-coupled receptor., Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, Leslie AG, Tate CG, Schertler GF, Nature. 2008 Jul 24;454(7203):486-91. Epub 2008 Jun 25. PMID:18594507
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2vt4 is a 4 chain structure with sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
See Also
Reference
- Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, Leslie AG, Tate CG, Schertler GF. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature. 2008 Jul 24;454(7203):486-91. Epub 2008 Jun 25. PMID:18594507 doi:nature07101
- Serrano-Vega MJ, Magnani F, Shibata Y, Tate CG. Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form. Proc Natl Acad Sci U S A. 2008 Jan 22;105(3):877-82. Epub 2008 Jan 11. PMID:18192400
Categories: Meleagris gallopavo | Baker, J G. | Edwards, P C. | Henderson, R. | Leslie, A G.W. | Moukhametzianov, R. | Schertler, G F.X. | Serrano-Vega, M J. | Tate, C G. | Warne, A. | 7tm receptor | Antagonist bound form | G protein coupled receptor | G-protein coupled receptor | Glycoprotein | Gpcr | Integral membrane protein | Lipoprotein | Membrane | Palmitate | Phosphoprotein | Receptor | Seven-helix receptor | Thermostabilising point mutation | Transducer | Transmembrane
