8WGC: Heterodimer of mGlu2 and mGlu4

heterodimer of mGlu2 and mGlu4 bound with mGlu2 agonist LY379268. Determined by electron microscopy at 5.95 Å resolution. Released 27 Nov 2024.

Method: Electron microscopy
Resolution: 5.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,193
Mol. weight: 192.41 kDa
Ligands: W92
Released: 27 Nov 2024

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

Secondary structure: helices and β-sheets

8WGC contains 87 α-helices and 63 β-strands across 2 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: 46 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	43-45	3	11
β-strand	49-55	7	11
β-strand	58-60	3	12
β-strand	67-70	4	12
α-helix	72-77	6
α-helix	78-91	14
β-strand	101-107	7	11
α-helix	112-119	8
α-helix	121-124	4
β-strand	150-154	5	11
α-helix	159-170	12
β-strand	176-178	3	11
α-helix	184-186	3
β-strand	195-197	3	11
α-helix	203-215	13
β-strand	220-226	7	13
α-helix	229-245	17
β-strand	249-256	8	13
α-helix	260-261	2
α-helix	264-272	9
α-helix	273-275	3
β-strand	280-284	5	13
α-helix	287-299	13
β-strand	307-310	4	13
α-helix	319-321	3
α-helix	325-328	4
β-strand	332-336	5	13
α-helix	342-348	7
α-helix	353-355	3
α-helix	362-369	8
β-strand	372-373	2	14
β-strand	386-387	2	14
α-helix	388	1
β-strand	394	1	15
β-strand	398	1	15
α-helix	406-427	22
α-helix	436-438	3
α-helix	443-451	9
β-strand	455-456	2	16
β-strand	462-463	2	16
α-helix	470-473	4
β-strand	474-483	10	13
β-strand	486-496	11	13
β-strand	499-501	3	13
α-helix	503-505	3
β-strand	508	1	17
β-strand	512	1	17
α-helix	523-525	3
β-strand	528-533	6	18
β-strand	536-544	9	18
β-strand	549-553	5	19
β-strand	556-559	4	19
α-helix	560-561	2
β-strand	564-566	3	20
α-helix	567	1
β-strand	573-575	3	20
α-helix	576-577	2
β-strand	578-579	2	21
α-helix	586-611	26
α-helix	616-619	4
α-helix	623-640	18
α-helix	641-644	4
α-helix	647	1
α-helix	649-652	4
α-helix	657-682	26
α-helix	683-685	3
α-helix	691	1
α-helix	696-720	25
β-strand	725-728	4	21
α-helix	729-732	4
α-helix	737-739	3
β-strand	742-746	5	21
α-helix	752-771	20
α-helix	772-776	5
α-helix	779-784	6
α-helix	785-805	21
α-helix	814-833	20
α-helix	834-838	5
α-helix	839-847	9

Chain D: 41 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	26-27	2	1
β-strand	32-33	2	2
β-strand	36-38	3	1
β-strand	41-43	3	3
β-strand	50-53	4	3
α-helix	54	1
α-helix	55-60	6
α-helix	61-74	14
β-strand	84-85	2	2
β-strand	87-90	4	1
α-helix	95-101	7
α-helix	102-105	4
β-strand	139-141	3	1
α-helix	145-154	10
α-helix	155-158	4
β-strand	162-164	3	1
α-helix	170-173	4
β-strand	181-183	3	1
α-helix	189-201	13
β-strand	206-212	7	4
α-helix	215-230	16
β-strand	234-241	8	4
α-helix	247-257	11
β-strand	265-268	4	4
α-helix	274-277	4
α-helix	278-280	3
β-strand	290-293	4	4
α-helix	301-303	3
β-strand	315-319	5	4
α-helix	325-332	8
α-helix	345-352	8
α-helix	378-399	22
α-helix	415-418	4
α-helix	419-423	5
β-strand	429	1	5
α-helix	430	1
β-strand	440	1	5
β-strand	453-459	7	4
β-strand	467-474	8	4
β-strand	478-480	3	4
α-helix	482-484	3
α-helix	495-497	3
α-helix	502-505	4
β-strand	508-511	4	6
β-strand	521-524	4	6
α-helix	525-526	2
β-strand	530-533	4	7
β-strand	536-538	3	7
β-strand	544-546	3	8
β-strand	553-555	3	8
α-helix	556-557	2
β-strand	558	1	9
α-helix	569-586	18
α-helix	589-593	5
α-helix	596-599	4
α-helix	601-620	20
α-helix	629-632	4
α-helix	642	1
α-helix	643-647	5
α-helix	648-660	13
α-helix	676-695	20
α-helix	696-699	4
β-strand	708	1	10
β-strand	717	1	9
β-strand	718	1	10
α-helix	725-729	5
α-helix	736-748	13
α-helix	755-757	3
α-helix	758-774	17
α-helix	777-783	7
α-helix	787-819	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 2	D	protein	854	Homo sapiens	Q14416 (AlphaFold model)
Metabotropic glutamate receptor 4	A	protein	880	Homo sapiens	Q14833 (AlphaFold model)

Sequence of entity 1 (D), FASTA

>8WGC_1 Metabotropic glutamate receptor 2 (chains D)
EGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHL
LPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITG
VIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEI
LRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALL
QKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIE
LASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKI
MFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTH
NEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPAS
RCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQ
EYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYC
MTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPAS
QVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLL
IALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSV
SLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTV
CNGREVVDSTTSSL

Sequence of entity 2 (A), FASTA

>8WGC_2 Metabotropic glutamate receptor 4 (chains A)
KPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINND
PDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVG
VIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDI
VRALKWNYVSTVASEGSYGESGVEAFIQKSREDGGVCIAQSVKIPREPKAGEFDKIIRRL
LETSNARAVIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAV
TILPKRMSVRGFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTNRE
RIGQDSAYEQEGKVQFVIDAVYAMGHALHAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRN
VNFSGIAGNPVTFNENGDAPGRYDIYQYQLRNDSAEYKVIGSWTDHLHLRIERMHWPGSG
QQLPRSICSLPCQPGERKKTVKGMPCCWHCEPCTGYQYQVDRYTCKTCPYDMRPTENRTG
CRPIPIIKLEWGSPWAVLPLFLAVVGIAATLFVVITFVRYNDTPIVKASGRELSYVLLAG
IFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPR
FISPASQLAITFSLISLQLLGICVWFVVDPSHSVVDFQDQRTLDPRFARGVLKCDISDLS
LICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSA
DKLYIQTTTLTVSVSLSASVSLGMLYMPKVYIILFHPEQNVPKRKRSLKAVVTAATMSNK
FTQKGNFRPNGEAKSELCENLEAPALATKQTYVTYTNHAI

Ligands and cofactors

ID	Name	Formula	Copies
W92	(1R,4R,5S,6R)-4-azanyl-2-oxabicyclo[3.1.0]hexane-4,6-dicarboxylic acid	C7 H9 N O5	1

Primary citation

Structural basis of orientated asymmetry in a mGlu heterodimer. Huang, W., Jin, N., Guo, J. et al. Nat Commun (2024) 15:10345-10345. DOI 10.1038/s41467-024-54744-7 · PubMed

Other PDB entries of the same protein (UniProt Q14416 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4XAQ 2.21 Å, mGluR2 ECD and mGluR3 ECD with ligands
4XAS 2.35 Å, mGluR2 ECD ligand complex
7EPE 2.5 Å, Crystal structure of mGlu2 bound to NAM563
5CNJ 2.65 Å, mGlur2 with glutamate analog
5CNI 2.69 Å, mGlu2 with Glutamate
7EPF 2.7 Å, Crystal structure of mGlu2 bound to NAM597
5KZN 2.8 Å, Metabotropic Glutamate Receptor
5KZQ 2.8 Å, Metabotropic Glutamate Receptor in complex with antagonist…
8JCU 2.8 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 (dimerization mode I)
8JD2 2.8 Å, Cryo-EM structure of G protein-free mGlu2-mGlu3 heterodimer in Acc state
8JCY 2.9 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and…
8JD4 2.9 Å, Cryo-EM structure of G protein-free mGlu2-mGlu4 heterodimer in Acc state

Browse structure collections

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