6UMG

Crystal structure of erenumab Fab bound to the extracellular domain of CGRP receptor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.245 
  • R-Value Observed: 0.247 

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This is version 1.2 of the entry. See complete history


Literature

Molecular Insight into Recognition of the CGRPR Complex by Migraine Prevention Therapy Aimovig (Erenumab).

Garces, F.Mohr, C.Zhang, L.Huang, C.S.Chen, Q.King, C.Xu, C.Wang, Z.

(2020) Cell Rep 30: 1714

  • DOI: https://doi.org/10.1016/j.celrep.2020.01.029
  • Primary Citation of Related Structures:  
    6UMG, 6UMH, 6UMI, 6UMJ

  • PubMed Abstract: 

    Calcitonin-gene-related peptide (CGRP) plays a key role in migraine pathophysiology. Aimovig (erenumab; erenumab-aooe in the United States) is the only US Food and Drug Administration (FDA)-approved monoclonal antibody (mAb) therapy against the CGRP receptor (CGRPR) for the prevention of migraine. Aimovig is also the first FDA-approved mAb against a G-protein-coupled receptor (GPCR). Here, we report the architecture and functional attributes of erenumab critical for its potent antagonism against CGRPR. The crystal structure of erenumab in complex with CGRPR reveals a direct ligand-blocking mechanism, enabled by a remarkable 21-residue-long complementary determining region (CDR)-H3 loop, which adopts a tyrosine-rich helix-turn tip and projects into the deep interface of the calcitonin receptor-like receptor (CLR) and RAMP1 subunits of CGRPR. Furthermore, erenumab engages with residues specific to CLR and RAMP1, providing the molecular basis for its exquisite selectivity. Such structural insights reveal the drug action mechanism of erenumab and shed light on developing antibody therapeutics targeting GPCRs.


  • Organizational Affiliation

    Department of Therapeutic Discovery, Amgen Research, Amgen, Thousand Oaks, CA 91320, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
erenumab Fab heavy chain, IgG1A [auth H],
E [auth h]
237Homo sapiensMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
erenumab Fab light chain, IgG1B [auth L],
F [auth l]
216Homo sapiensMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Calcitonin gene-related peptide type 1 receptorC,
G [auth c]
139Homo sapiensMutation(s): 0 
Gene Names: CALCRLCGRPR
UniProt & NIH Common Fund Data Resources
Find proteins for Q16602 (Homo sapiens)
Explore Q16602 
Go to UniProtKB:  Q16602
PHAROS:  Q16602
GTEx:  ENSG00000064989 
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UniProt GroupQ16602
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Receptor activity-modifying protein 1D [auth R],
H [auth r]
120Homo sapiensMutation(s): 0 
Gene Names: RAMP1
UniProt & NIH Common Fund Data Resources
Find proteins for O60894 (Homo sapiens)
Explore O60894 
Go to UniProtKB:  O60894
PHAROS:  O60894
GTEx:  ENSG00000132329 
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UniProt GroupO60894
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.245 
  • R-Value Observed: 0.247 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.464α = 90
b = 112.52β = 91.84
c = 77.254γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
DENZOdata reduction
HKL-2000data reduction
SCALEPACKdata scaling
HKL-2000data scaling
PHASERphasing
MOLREPphasing
REFMACrefinement
Cootmodel building
PHENIXmodel building
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 2020-02-12 
  • Deposition Author(s): Mohr, C.

Revision History  (Full details and data files)

  • Version 1.0: 2020-02-12
    Type: Initial release
  • Version 1.1: 2020-02-26
    Changes: Database references
  • Version 1.2: 2023-10-11
    Changes: Data collection, Database references, Refinement description