8F0J: Calcitonin Receptor

Calcitonin Receptor in complex with Gs and Pramlintide analogue peptide San45. Determined by electron microscopy at 2.0 Å resolution. Released 2 Aug 2023.

Method: Electron microscopy
Resolution: 2.0 Å
Organisms: Homo sapiens, Lama glama
Chains: 6
Atoms: 9,678
Mol. weight: 176.48 kDa
Ligands: PTY, NAG, D6M, P42
Released: 2 Aug 2023

Explore 8F0J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8F0J contains 43 α-helices and 57 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: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	12-39	28
β-strand	41-47	7	6
α-helix	53-59	7
β-strand	207-214	8	6
β-strand	217-224	8	6
α-helix	234-238	5
β-strand	243-249	7	6
α-helix	265-278	14
α-helix	280-282	3
β-strand	286-292	7	6
α-helix	294-303	10
α-helix	308-311	4
α-helix	313-317	5
α-helix	332-351	20
β-strand	359-363	5	6
α-helix	370-390	21

Chain B: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	3-25	23
α-helix	30-33	4
α-helix	38-39	2
β-strand	47-51	5	7
β-strand	58-63	6	8
β-strand	69-74	6	8
β-strand	78-83	6	8
β-strand	89-94	6	8
β-strand	100-105	6	9
β-strand	111-116	6	9
β-strand	121-125	5	9
β-strand	134-139	6	9
β-strand	146-151	6	10
β-strand	156-161	6	10
β-strand	166-170	5	10
β-strand	175-180	6	10
β-strand	187-192	6	11
β-strand	198-203	6	11
β-strand	207-212	6	11
β-strand	218-223	6	11
β-strand	229-234	6	12
β-strand	240-245	6	12
β-strand	250-254	5	12
β-strand	259-264	6	12
β-strand	273-278	6	13
β-strand	284-289	6	13
β-strand	294-298	5	13
β-strand	304-308	5	13
β-strand	315-320	6	7
β-strand	327-331	5	7
β-strand	336-339	4	7

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	9-23	15
α-helix	30-43	14
α-helix	53-55	3

Chain N: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	14
β-strand	10-12	3	15
β-strand	18-25	8	14
α-helix	29-31	3
β-strand	34-39	6	15
β-strand	45-51	7	15
β-strand	58-60	3	15
α-helix	62-64	3
β-strand	68-73	6	14
β-strand	78-83	6	14
α-helix	88-90	3
β-strand	92-98	7	15
β-strand	118	1	15
β-strand	122-126	5	15

Chain P: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	5-7	3
α-helix	8-18	11
α-helix	28-31	4

Chain R: 21 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	39-61	23
β-strand	71-72	2	1
α-helix	73-74	2
β-strand	75-76	2	2
β-strand	81-82	2	2
β-strand	85-86	2	1
β-strand	89-94	6	3
β-strand	102	1	4
β-strand	107-112	6	3
β-strand	118	1	3
β-strand	120	1	5
β-strand	127	1	5
β-strand	130	1	3
α-helix	132-134	3
β-strand	135	1	4
α-helix	139-172	34
α-helix	174-176	3
α-helix	179-200	22
α-helix	201-205	5
α-helix	209-214	6
α-helix	217-248	32
α-helix	260-263	4
α-helix	264-268	5
α-helix	271-283	13
α-helix	288-290	3
α-helix	296-298	3
α-helix	299-329	31
α-helix	334-352	19
α-helix	355-358	4
α-helix	366-381	16
α-helix	383-388	6
α-helix	389-393	5
α-helix	396-407	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
pramlintide analogue San45	P	protein	38	Homo sapiens	P10997 (AlphaFold model)
Calcitonin receptor	R	protein	501	Homo sapiens	P30988 (AlphaFold model)
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	A	protein	394	Homo sapiens	P63092 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	350	Homo sapiens	P62873 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Homo sapiens	P59768
nanobody 35	N	protein	138	Lama glama

Sequence of entity 1 (P), FASTA

>8F0J_1 pramlintide analogue San45 (chains P)
KCNTATCATQRLANFLVHSSKNFGPILPPTNVGSNTYX

Sequence of entity 2 (R), FASTA

>8F0J_2 Calcitonin receptor (chains R)
MKTIIALSYIFCLVFADYKDDDDLEVLFQGPAAFSNQTYPTIEPKPFLYVVGRKKMMDAQ
YKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYC
DEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVF
FRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMAC
NYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLS
VETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLL
GIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQ
WNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQELRNEPANNQGEESAEIIPLNIIEQES
SAPAGLEVLFQGPHHHHHHHH

Sequence of entity 3 (A), FASTA

>8F0J_3 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains A)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKNTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQAALKLFDSIWNNKWLRDTSVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL

Sequence of entity 4 (B), FASTA

>8F0J_4 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRT
LRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGN
YVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWD
IETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDIN
AICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYD
DFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 5 (G), FASTA

>8F0J_5 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Sequence of entity 6 (N), FASTA

>8F0J_6 nanobody 35 (chains N)
QVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVRQAPGKGLEWVSDISQSGASISY
TGSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCARCPAPFTRDCFDVTSTTYAYRGQ
GTQVTVSSHHHHHHEPEA

Ligands and cofactors

ID	Name	Formula	Copies
PTY	Phosphatidylethanolamine	C40 H80 N O8 P	3
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
D6M	N-hexadecanoyl-L-glutamic acid	C21 H39 N O5	1
P42	(2S)-2-{[(1R)-1-hydroxyhexadecyl]oxy}-3-{[(1R)-1-hydroxyoctadecyl]oxy}propyl…	C42 H88 N O8 P	1
Y01	Cholesterol hemisuccinate	C31 H50 O4	2
PLM	Palmitic acid	C16 H32 O2	8

Primary citation

Structural insight into selectivity of amylin and calcitonin receptor agonists. Cao, J., Belousoff, M.J., Gerrard, E. et al. Nat Chem Biol (2024) 20:162-169. DOI 10.1038/s41589-023-01393-4 · PubMed

Other PDB entries of the same protein (UniProt P10997 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8YG2 1.25 Å, Crystal structure of amyloidogenic peptide Piv-NFGAIL-NH2 from Islet Amyloid Polypeptide
5KO0 1.4 Å, Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED
3FPO 1.5 Å, HSSNNF segment from Islet Amyloid Polypeptide (IAPP or Amylin)
3FTK 1.5 Å, NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form
3FTL 1.6 Å, NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), dehydrated crystal form
3FTR 1.61 Å, Structure of an amyloid forming peptide SSTNVG from IAPP (alternate polymorph)
3DG1 1.66 Å, Segment SSTNVG derived from IAPP
3G7W 1.75 Å, Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding…
3FTH 1.84 Å, NFLVHSS segment from Islet Amyloid Polypeptide (IAPP or Amylin)
3FR1 1.85 Å, NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)
3G7V 1.86 Å, Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein
9CC5 1.87 Å, De novo design of high-affinity protein binders to bio active peptide Amylin

Browse structure collections

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