8JSR: Anamorelin-bound ghrelin receptor and Gq complex

Cryo-EM structure of the anamorelin-bound ghrelin receptor and Gq complex. Determined by electron microscopy at 2.9 Å resolution. Released 22 Jan 2025.

Method: Electron microscopy
Resolution: 2.9 Å
Organisms: Homo sapiens, Mus musculus, Lama glama
Chains: 6
Atoms: 10,001
Mol. weight: 193.04 kDa
Ligands: UYI
Released: 22 Jan 2025

Explore 8JSR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8JSR contains 39 α-helices and 70 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-32	26
β-strand	34-40	7	2
α-helix	46-53	8
α-helix	54-56	3
β-strand	184-190	7	2
β-strand	195-201	7	2
α-helix	211-215	5
β-strand	220-226	7	2
α-helix	233-245	13
β-strand	253-259	7	2
α-helix	261-270	10
α-helix	275-277	3
α-helix	280-282	3
α-helix	293-294	2
α-helix	299-318	20
β-strand	326-330	5	2
α-helix	338-357	20

Chain B: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	4-24	21
α-helix	30-33	4
α-helix	38-39	2
β-strand	46-51	6	3
β-strand	58-63	6	4
β-strand	69-74	6	4
β-strand	78-83	6	4
β-strand	88-94	7	4
β-strand	100-105	6	5
β-strand	111-116	6	5
β-strand	121-125	5	5
β-strand	134-139	6	5
β-strand	146-151	6	6
β-strand	156-161	6	6
β-strand	166-170	5	6
β-strand	175-180	6	6
β-strand	187-192	6	7
β-strand	198-203	6	7
β-strand	208-212	5	7
β-strand	217-221	5	7
β-strand	229-234	6	8
β-strand	240-245	6	8
β-strand	250-254	5	8
β-strand	259-264	6	8
β-strand	273-278	6	9
β-strand	284-289	6	9
β-strand	294-298	5	9
β-strand	303-308	6	9
β-strand	315-320	6	3
β-strand	327-331	5	3
β-strand	336-340	5	3

Chain C: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	10
β-strand	11-12	2	11
β-strand	18-25	8	10
α-helix	29-31	3
β-strand	33-39	7	12
β-strand	45-51	7	12
β-strand	58-60	3	12
α-helix	62-64	3
β-strand	69-73	5	10
β-strand	78-83	6	10
α-helix	88-90	3
β-strand	92-99	8	12
β-strand	111	1	12
β-strand	115-117	3	12
β-strand	118-119	2	11
α-helix	138-139	2
β-strand	140-141	2	13
β-strand	146-148	3	14
β-strand	155-161	7	13
β-strand	174-179	6	14
β-strand	186-190	5	14
β-strand	194-195	2	14
α-helix	196	1
β-strand	203-207	5	13
β-strand	211-216	6	13
α-helix	221-223	3
β-strand	225-231	7	14
α-helix	237	1
β-strand	239	1	14
β-strand	243-246	4	14

Chain G: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	7-23	17
α-helix	30-43	14
α-helix	45-47	3
α-helix	53-55	3

Chain N: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	15
β-strand	10-11	2	16
β-strand	17-25	9	15
α-helix	29-31	3
β-strand	34-39	6	16
β-strand	45-51	7	16
β-strand	58-60	3	16
β-strand	68-73	6	15
β-strand	78-84	7	15
α-helix	88-90	3
β-strand	92-98	7	16
β-strand	118	1	16
β-strand	122-125	4	16

Chain R: 12 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	40-70	31
α-helix	77-94	18
α-helix	96-104	9
α-helix	113-146	34
α-helix	148-154	7
α-helix	157-174	18
α-helix	178-181	4
β-strand	182-186	5	1
β-strand	196-200	5	1
α-helix	202-207	6
α-helix	209-240	32
α-helix	259-288	30
α-helix	297-324	28
α-helix	330-337	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth hormone secretagogue receptor type 1	R	protein	523	Homo sapiens	Q92847 (AlphaFold model)
Engineered G-alpha-q	A	protein	361	Homo sapiens
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	388	Homo sapiens	P62873 (AlphaFold model)
scFv16	C	protein	259	Mus musculus
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Homo sapiens	P59768 (AlphaFold model)
Nb35	N	protein	129	Lama glama

Sequence of entity 1 (R), FASTA

>8JSR_1 Growth hormone secretagogue receptor type 1 (chains R)
WNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGN
LLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQF
VSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVL
VGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWR
RRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQIS
QYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTE
SSINTVFTLEDFVGDWEQTAAYNLDQVLEQGGVSSLLQNLAVSVTPIQRIVRSGENALKI
DIHVIIPYEGLSADQMAQIEEVFKVVYPVDDHHFKVILPYGTLVIDGVTPNMLNYFGRPY
EGIAVFDGKKITVTGTLWNGNKIIDERLITPDGSMLFRVTINS

Sequence of entity 2 (A), FASTA

>8JSR_2 Engineered G-alpha-q (chains A)
MGCTLSAEDKAAVERSKMIEKQLQKDKQVYRRTLRLLLLGADNSGKSTIVKQMRIYHVNG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQEALNDF
KSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPR
VTRAKYFIRKEFVDISTASGDGRHICYPHFTCSVDTENARRIFNDCKDIILQMNLREYNL
V

Sequence of entity 3 (B), FASTA

>8JSR_3 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHHHHHLEVLFQGPGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNID
PVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSS
WVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIV
TSSGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMC
RQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSF
SKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKI
WNGSSGGGGSGGGGSSGVSGWRLFKKIS

Sequence of entity 4 (C), FASTA

>8JSR_4 scFv16 (chains C)
DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY
ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS
SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR
PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG
AGTKLELKAAAHHHHHHHH

Sequence of entity 5 (G), FASTA

>8JSR_5 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Sequence of entity 6 (N), FASTA

>8JSR_6 Nb35 (chains N)
MQVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVRQAPGKGLEWVSDISQSGASIS
YTGSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCARCPAPFTRDCFDVTSTTYAYRG
QGTQVTVSS

Ligands and cofactors

ID	Name	Formula	Copies
UYI	Anamorelin	C31 H42 N6 O3	1

Primary citation

The structure and function of the ghrelin receptor coding for drug actions. Shiimura, Y., Im, D., Tany, R. et al. Nat Struct Mol Biol (2025) 32:531-542. DOI 10.1038/s41594-024-01481-6 · PubMed

Other PDB entries of the same protein (UniProt Q92847 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9UY3 2.52 Å, Anamorelin bound growth hormone secretagogue receptor in complex with Gq
9V2N 2.63 Å, Macimorelin bound growth hormone secretagogue receptor in complex with Gq
7NA7 2.7 Å, Structures of human ghrelin receptor-Gi complexes with ghrelin and a synthetic agonist
7NA8 2.7 Å, Structures of human ghrelin receptor-Gi complexes with ghrelin and a synthetic agonist
7W2Z 2.8 Å, Cryo-EM structure of the ghrelin-bound human ghrelin receptor-Go complex
7F9Y 2.9 Å, ghrelin-bound ghrelin receptor in complex with Gq
7F83 2.94 Å, Crystal Structure of a receptor in Complex with inverse agonist
7F9Z 3.2 Å, GHRP-6-bound ghrelin receptor in complex with Gq
6KO5 3.3 Å, Complex structure of Ghrelin receptor with Fab
8ZZO Structural Model of Ghrelin Bound to its G Protein-Coupled Receptor

Browse structure collections

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