› 4rwg

X-ray diffraction
2.44Å resolution

Crystal structure of the CLR:RAMP1 extracellular domain heterodimer with bound high affinity CGRP analog

Released:
DOI: 10.2210/pdb4rwg/pdb
PDB 4rwg coloured by chain and viewed from the front.
PDB 4rwg coloured by chain and viewed from the side.
PDB 4rwg coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.
Booe JM, Walker CS, Barwell J, Kuteyi G, Simms J, Jamaluddin MA, Warner ML, Bill RM, Harris PW, Brimble MA, Poyner DR, Hay DL, Pioszak AA
OpenAccess logo Mol Cell 58 1040-52 (2015)
PMID: 25982113

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Calcitonin gene-related peptide type 1 receptor; Maltose/maltodextrin-binding periplasmic protein; Receptor activity-modifying protein 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 593 amino acids
Theoretical weight: 66.3 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 25-392; Coverage: 99%)
  • Canonical: O60894 (Residues: 23-108; Coverage: 67%)
  • Canonical: Q16602 (Residues: 31-144; Coverage: 26%)
Gene names: CALCRL, CGRPR, JW3994, RAMP1, b4034, malE
Sequence domains:
CGRP analog Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 12 amino acids
Theoretical weight: 1.19 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 172.806Å b: 104.623Å c: 136.483Å
α: 90° β: 122.43° γ: 90°
R-values:
R R work R free
0.202 0.2 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 review citations

Calcitonin and Bone Physiology: In Vitro, In Vivo, and Clinical Investigations.
Xie et al. (2020)
10 more

2 mentions without citation

Structure-function analyses reveal a triple β-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design.
Roehrkasse et al. (2018)
1 more