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Structure paper

TitleStructural insights into CXCR4 modulation and oligomerization.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateSep 23, 2024
AuthorsKei Saotome / Luke L McGoldrick / Jo-Hao Ho / Trudy F Ramlall / Sweta Shah / Michael J Moore / Jee Hae Kim / Raymond Leidich / William C Olson / Matthew C Franklin /
PubMed AbstractActivation of the chemokine receptor CXCR4 by its chemokine ligand CXCL12 regulates diverse cellular processes. Previously reported crystal structures of CXCR4 revealed the architecture of an ...Activation of the chemokine receptor CXCR4 by its chemokine ligand CXCL12 regulates diverse cellular processes. Previously reported crystal structures of CXCR4 revealed the architecture of an inactive, homodimeric receptor. However, many structural aspects of CXCR4 remain poorly understood. Here, we use cryo-electron microscopy to investigate various modes of human CXCR4 regulation. CXCL12 activates CXCR4 by inserting its N terminus deep into the CXCR4 orthosteric pocket. The binding of US Food and Drug Administration-approved antagonist AMD3100 is stabilized by electrostatic interactions with acidic residues in the seven-transmembrane-helix bundle. A potent antibody blocker, REGN7663, binds across the extracellular face of CXCR4 and inserts its complementarity-determining region H3 loop into the orthosteric pocket. Trimeric and tetrameric structures of CXCR4 reveal modes of G-protein-coupled receptor oligomerization. We show that CXCR4 adopts distinct subunit conformations in trimeric and tetrameric assemblies, highlighting how oligomerization could allosterically regulate chemokine receptor function.
External linksNat Struct Mol Biol / PubMed:39313635
MethodsEM (single particle)
Resolution2.72 - 3.38 Å
Structure data

41888

8u4n

EMDB-41888, PDB-8u4n:
Structure of Apo CXCR4/Gi complex
Method: EM (single particle) / Resolution: 2.72 Å

41889

8u4o

EMDB-41889, PDB-8u4o:
Structure of CXCL12-bound CXCR4/Gi complex
Method: EM (single particle) / Resolution: 3.29 Å

41890

8u4p

EMDB-41890, PDB-8u4p:
Structure of AMD3100-bound CXCR4/Gi complex
Method: EM (single particle) / Resolution: 3.15 Å

41891

8u4q

EMDB-41891, PDB-8u4q:
Structure of REGN7663 Fab-bound CXCR4/Gi complex
Method: EM (single particle) / Resolution: 3.36 Å

41892

8u4r

EMDB-41892, PDB-8u4r:
Structure of REGN7663-Fab bound CXCR4
Method: EM (single particle) / Resolution: 3.1 Å

41893

8u4s

EMDB-41893, PDB-8u4s:
Structure of trimeric CXCR4 in complex with REGN7663 Fab
Method: EM (single particle) / Resolution: 3.35 Å

41894

8u4t

EMDB-41894, PDB-8u4t:
Structure of tetrameric CXCR4 in complex with REGN7663 Fab
Method: EM (single particle) / Resolution: 3.38 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL


ChemComp, No image

ChemComp-VH6:
Unknown entry

ChemComp-D21:
(2R)-1-(hexadecanoyloxy)-3-(phosphonooxy)propan-2-yl (9Z)-octadec-9-enoate

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / GPCR / chemokine receptor / chemokine / plerixafor / AMD3100 / SIGNALING PROTEIN/IMMUNE SYSTEM / antibody / Fab / SIGNALING PROTEIN-IMMUNE SYSTEM complex / trimer / oligomer / tetramer

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