8XWA: CXCR2

Structure of CXCR2 bound to CXCL1 (Ligand-receptor focused map). Determined by electron microscopy at 3.48 Å resolution. Released 15 Jan 2025.

Method: Electron microscopy
Resolution: 3.48 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,301
Mol. weight: 62.45 kDa
Released: 15 Jan 2025

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

Secondary structure: helices and β-sheets

8XWA contains 20 α-helices and 16 β-strands across 3 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 D: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	15	1	2
α-helix	20-22	3
β-strand	23-29	7	2
β-strand	32	1	3
β-strand	35	1	3
β-strand	39-44	6	2
β-strand	49-52	4	2
α-helix	57-67	11

Chain E: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	2
α-helix	20-22	3
β-strand	23-29	7	2
β-strand	32	1	4
β-strand	35	1	4
β-strand	39-44	6	2
β-strand	49-52	4	2
α-helix	57-67	11

Chain R: 16 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	45-75	31
α-helix	82-99	18
α-helix	101-110	10
α-helix	116-148	33
α-helix	154-159	6
α-helix	162-176	15
α-helix	178-182	5
β-strand	184-187	4	5
β-strand	192	1	1
β-strand	195-198	4	5
α-helix	204-211	8
α-helix	213-216	4
α-helix	217-221	5
α-helix	222-238	17
α-helix	246-278	33
α-helix	286-304	19
α-helix	306-310	5
α-helix	311-315	5
α-helix	319-329	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth-regulated alpha protein	D, E	protein	73	Homo sapiens	P09341 (AlphaFold model)
C-X-C chemokine receptor type 2	R	protein	416	Homo sapiens	P25025 (AlphaFold model)

Sequence of entity 1 (D, E), FASTA

>8XWA_1 Growth-regulated alpha protein (chains D, E)
ASVATELRCQCLQTLQGIHPKNIQSVNVKSPGPHCAQTEVIATLKNGRKACLNPASPIVK
KIIEKMLNSDKSN

Sequence of entity 2 (R), FASTA

>8XWA_2 C-X-C chemokine receptor type 2 (chains R)
MGKTIIALSYIFCLVFADYKDDDDAANFTPVNGSSGNQSVRLVTSSSLEVLFQGPGSEDF
NMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLL
GNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSL
LKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFR
RTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMG
QKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILGI
LHSCLNPLIYAFIGQKFRHGLLKILAIHGLISKDSLPKDSRPSFVGSSSGHTSTTL

Primary citation

Molecular basis of promiscuous chemokine binding and structural mimicry at the C-X-C chemokine receptor, CXCR2. Saha, S., Sano, F.K., Sharma, S. et al. Mol Cell (2025) 85:976-988.e9. DOI 10.1016/j.molcel.2025.01.024 · PubMed

Other PDB entries of the same protein (UniProt P09341 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9EJC 2.98 Å, Cryo-EM Structure of CXCL1-KSHV ORF74-Gi-scFv16 Complex
8K4O 3.01 Å, Cryo-EM structure of Kaposi's Sarcoma-Associated Herpesvirus-G Protein-Coupled Receptor…
8XWV 3.07 Å, Structure of CXCR2 bound to CXCL1 (CXCR2-CXCL1-Go Full map)
1MGS The solution structure of melanoma growth stimulating activity
1MSG Solution structure of gro(slash)melanoma growth stimulatory activity determined by 1H…
1MSH Solution structure of gro(slash)melanoma growth stimulatory activity determined by 1H…
1ROD Chimeric protein of interleukin 8 and human melanoma growth stimulating activity…

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