PDBsum entry 6wwz

Membrane protein

PDB id: 6wwz

Contents

Protein chains

338 a.a.

66 a.a.

56 a.a.

210 a.a.

231 a.a.

310 a.a.

PDB id:

6wwz

Name:

Membrane protein

Title:

Cryo-em structure of the human chemokine receptor ccr6 in complex with ccl20 and a go protein

Structure:

Guanine nucleotide-binding protein g(i)/g(s)/g(t) subunit beta-1. Chain: b. Synonym: transducin beta chain 1. Engineered: yes. C-c motif chemokine 20. Chain: c. Synonym: beta-chemokine exodus-1,cc chemokine larc,liver and activation-regulated chemokine,macrophage inflammatory protein 3

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: gnb1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Homo sapiens. Human. Organism_taxid: 9606.

Authors:

D.J.Wasilko,Z.L.Johnson,M.Ammirati,S.Han,H.Wu

Key ref:

D.J.Wasilko et al. (2020). Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20. Nat Commun, 11, 3031. PubMed id: 32541785 DOI: 10.1038/s41467-020-16820-6

Date:

09-May-20 Release date: 24-Jun-20

Protein chain

P54311  (GBB1_RAT) -  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Rattus norvegicus

Seq: 340 a.a.

Struc: 338 a.a.

Protein chain

P78556  (CCL20_HUMAN) -  C-C motif chemokine 20 from Homo sapiens

Seq: 96 a.a.

Struc: 66 a.a.

Protein chain

P59768  (GBG2_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 from Homo sapiens

Seq: 71 a.a.

Struc: 56 a.a.

Protein chain

P09471  (GNAO_HUMAN) -  Guanine nucleotide-binding protein G(o) subunit alpha from Homo sapiens

Seq: 354 a.a.

Struc: 210 a.a.*

Protein chain

No UniProt id for this chain

Struc: 231 a.a.

Protein chain

P0ABE7  (C562_ECOLX) -  Soluble cytochrome b562 from Escherichia coli

Seq: 128 a.a.

Struc: 310 a.a.*

Protein chain

P51684  (CCR6_HUMAN) -  C-C chemokine receptor type 6 from Homo sapiens

Seq: 374 a.a.

Struc: 310 a.a.

* PDB and UniProt seqs differ at 165 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.3.6.5.- - ?????

DOI no: 10.1038/s41467-020-16820-6

Nat Commun 11:3031 (2020)

PubMed id: 32541785

Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20.

D.J.Wasilko, Z.L.Johnson, M.Ammirati, Y.Che, M.C.Griffor, S.Han, H.Wu.

ABSTRACT

Chemokines are important protein-signaling molecules that regulate various immune responses by activating chemokine receptors which belong to the G protein-coupled receptor (GPCR) superfamily. Despite the substantial progression of our structural understanding of GPCR activation by small molecule and peptide agonists, the molecular mechanism of GPCR activation by protein agonists remains unclear. Here, we present a 3.3-Å cryo-electron microscopy structure of the human chemokine receptor CCR6 bound to its endogenous ligand CCL20 and an engineered Go. CCL20 binds in a shallow extracellular pocket, making limited contact with the core 7-transmembrane (TM) bundle. The structure suggests that this mode of binding induces allosterically a rearrangement of a noncanonical toggle switch and the opening of the intracellular crevice for G protein coupling. Our results demonstrate that GPCR activation by a protein agonist does not always require substantial interactions between ligand and the 7TM core region.