7VV4: Mas-related G-protein coupled receptor member X2

Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with linear cortistatin-14, local. Determined by electron microscopy at 2.97 Å resolution. Released 1 Dec 2021.

Method: Electron microscopy
Resolution: 2.97 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,181
Mol. weight: 39.24 kDa
Ligands: CLR
Released: 1 Dec 2021

Explore 7VV4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7VV4 contains 19 α-helices and 0 β-strands across 1 chain. 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 R: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	28-53	26
α-helix	54-58	5
α-helix	65-90	26
α-helix	91-95	5
α-helix	105-132	28
α-helix	134-135	2
α-helix	136-140	5
α-helix	145-167	23
α-helix	177-212	36
α-helix	218-231	14
α-helix	232-236	5
α-helix	237-240	4
α-helix	241-246	6
α-helix	247-250	4
α-helix	253-255	3
α-helix	256-260	5
α-helix	261-276	16
α-helix	277-281	5
α-helix	282-284	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mas-related G-protein coupled receptor member X2	R	protein	330	Homo sapiens	Q96LB1 (AlphaFold model)
circular cortistatin-14	L	protein	14	Homo sapiens	O00230 (AlphaFold model)

Sequence of entity 1 (R), FASTA

>7VV4_1 Mas-related G-protein coupled receptor member X2 (chains R)
MDPTTPAWGTESTTVNGNDQALLLLCGKETLIPVFLILFIALVGLVGNGFVLWLLGFRMR
RNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSISINFPSFFTTVMTCAYLAGLSML
STVSTERCLSVLWPIWYRCRRPRHLSAVVCVLLWALSLLLSILEGKFCGFLFSDGDSGWC
QTFDFITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFG
IQWFLILWIWKDSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWRLQQPILKLAL
QRALQDIAEVDHSEGCFRQGTPEMSRSSLV

Sequence of entity 2 (L), FASTA

>7VV4_2 circular cortistatin-14 (chains L)
PCKNFFWKTFSSCK

Ligands and cofactors

ID	Name	Formula	Copies
CLR	Cholesterol	C27 H46 O	1

Primary citation

Structure, function and pharmacology of human itch receptor complexes. Yang, F., Guo, L., Li, Y. et al. Nature (2021) 600:164-169. DOI 10.1038/s41586-021-04077-y · PubMed

Other PDB entries of the same protein (UniProt Q96LB1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7S8L 2.45 Å, CryoEM structure of Gq-coupled MRGPRX2 with peptide agonist Cortistatin-14
7S8M 2.54 Å, CryoEM structure of Gi-coupled MRGPRX2 with peptide agonist Cortistatin-14
7S8O 2.58 Å, CryoEM structure of Gi-coupled MRGPRX2 with small molecule agonist (R)-Zinc-3573
7VV5 2.76 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with C48/80, state1
9WVX 2.8 Å, CryoEM structure of MRGPRX2 with peptide agonist DKD2
7VUY 2.84 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with PAMP-12. state1
7VUZ 2.89 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with PAMP-12, state2
7S8N 2.9 Å, CryoEM structure of Gq-coupled MRGPRX2 with small molecule agonist (R)-Zinc-3573
7VDH 2.9 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with C48/80, state2
7VV3 2.97 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with linear cortistatin-14
7VDM 2.98 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with substance P
7VDL 3.22 Å, Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with circular cortistatin-14

Browse structure collections

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