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8JIR

Cryo-EM structure of the GLP-1R/GCGR dual agonist SAR425899-bound human GLP-1R-Gs complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
P0005179molecular_functionhormone activity
P0005576cellular_componentextracellular region
R0004888molecular_functiontransmembrane signaling receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0004967molecular_functionglucagon receptor activity
R0005515molecular_functionprotein binding
R0005886cellular_componentplasma membrane
R0007166biological_processcell surface receptor signaling pathway
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007190biological_processactivation of adenylate cyclase activity
R0007204biological_processpositive regulation of cytosolic calcium ion concentration
R0007611biological_processlearning or memory
R0008016biological_processregulation of heart contraction
R0016020cellular_componentmembrane
R0017046molecular_functionpeptide hormone binding
R0019933biological_processcAMP-mediated signaling
R0031204biological_processpost-translational protein targeting to membrane, translocation
R0038023molecular_functionsignaling receptor activity
R0044508molecular_functionglucagon-like peptide 1 receptor activity
R0045776biological_processnegative regulation of blood pressure
R0045777biological_processpositive regulation of blood pressure
R0046879biological_processhormone secretion
R0071377biological_processcellular response to glucagon stimulus
R1990911biological_processresponse to psychosocial stress
Functional Information from PROSITE/UniProt
site_idPS00260
Number of Residues23
DetailsGLUCAGON Glucagon / GIP / secretin / VIP family signature. HSQGTFtSDLskqkeskaAQDFI
ChainResidueDetails
PHIS1-ILE23

site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDeya.CWpdGepgsfvnvsCP
ChainResidueDetails
RCYS62-PRO86

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV
ChainResidueDetails
RGLN394-VAL409

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04896
ChainResidueDetails
AGLY40
ASER47
AASP200
AASN259
AALA333

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER319

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: N-palmitoyl glycine => ECO:0000250|UniProtKB:P04896
ChainResidueDetails
AGLY2
RTYR252-ILE265
RCYS329-ARG348
RVAL405-SER463

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21044946
ChainResidueDetails
ACYS3

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
ALYS267

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ASER151

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ALEU175

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ATHR181

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG178

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Interaction with the endogenous ligand GLP-1 => ECO:0000269|PubMed:19861722
ChainResidueDetails
RARG121
RGLU128

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine => ECO:0000269|PubMed:21901419
ChainResidueDetails
RCYS341

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine => ECO:0000269|PubMed:21901419
ChainResidueDetails
RARG348

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22412906
ChainResidueDetails
RASN63
RASN82
RASN115

222926

PDB entries from 2024-07-24

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