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PDBsum entry 2y04
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PDB id:
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Receptor
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Title:
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Turkey beta1 adrenergic receptor with stabilising mutations and bound partial agonist salbutamol
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Structure:
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Beta-1 adrenergic receptor. Chain: a, b. Fragment: residues 33-368. Synonym: beta-1 adrenoreceptor, beta-1 adrenoceptor, beta-t. Engineered: yes. Mutation: yes. Other_details: residues 3-32 at the n-terminus and residues 244-271 of the third intracellular loop were deleted from the construct. The construct was truncated after residue 367 and a hexahis tag added.
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Source:
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Meleagris gallopavo. Turkey. Organism_taxid: 9103. Cell: erythrocyte. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five.
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Resolution:
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3.05Å
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R-factor:
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0.225
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R-free:
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0.255
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Authors:
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A.Warne,R.Moukhametzianov,J.G.Baker,R.Nehme,P.C.Edwards,A.G.W.Leslie, G.F.X.Schertler,C.G.Tate
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Key ref:
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T.Warne
et al.
(2011).
The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor.
Nature,
469,
241-244.
PubMed id:
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Date:
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30-Nov-10
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Release date:
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12-Jan-11
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PROCHECK
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Headers
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References
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P07700
(ADRB1_MELGA) -
Beta-1 adrenergic receptor from Meleagris gallopavo
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Seq:
Struc:
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483 a.a.
286 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 8 residue positions (black
crosses)
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Nature
469:241-244
(2011)
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PubMed id:
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The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor.
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T.Warne,
R.Moukhametzianov,
J.G.Baker,
R.Nehmé,
P.C.Edwards,
A.G.Leslie,
G.F.Schertler,
C.G.Tate.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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.
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Nature,
494,
185-194.
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F.Hausch,
and
F.Holsboer
(2012).
Structural biology: Snapshot of an activated peptide receptor.
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Nature,
490,
492-493.
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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.
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Nature,
490,
508-513.
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PDB code:
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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.
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Nature,
482,
237-240.
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PDB codes:
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F.Xu,
H.Wu,
V.Katritch,
G.W.Han,
K.A.Jacobson,
Z.G.Gao,
V.Cherezov,
and
R.C.Stevens
(2011).
Structure of an agonist-bound human A2A adenosine receptor.
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Science,
332,
322-327.
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PDB code:
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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.
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Nature,
474,
521-525.
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PDB codes:
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M.T.Tse
(2011).
G protein-coupled receptors: Crystallizing how agonists bind.
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Nat Rev Drug Discov,
10,
97.
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S.R.Sprang
(2011).
Cell signalling: Binding the receptor at both ends.
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Nature,
469,
172-173.
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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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Links
