6GKT

X-ray structure of a non-autocrystallizing galectin-10 variant, Gal10-Tyr69Glu


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.174 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Protein crystallization promotes type 2 immunity and is reversible by antibody treatment.

Persson, E.K.Verstraete, K.Heyndrickx, I.Gevaert, E.Aegerter, H.Percier, J.M.Deswarte, K.Verschueren, K.H.G.Dansercoer, A.Gras, D.Chanez, P.Bachert, C.Goncalves, A.Van Gorp, H.De Haard, H.Blanchetot, C.Saunders, M.Hammad, H.Savvides, S.N.Lambrecht, B.N.

(2019) Science 364

  • DOI: https://doi.org/10.1126/science.aaw4295
  • Primary Citation of Related Structures:  
    6GKQ, 6GKS, 6GKT, 6GKU, 6GLW, 6GLX, 6QRN

  • PubMed Abstract: 

    Although spontaneous protein crystallization is a rare event in vivo, Charcot-Leyden crystals (CLCs) consisting of galectin-10 (Gal10) protein are frequently observed in eosinophilic diseases, such as asthma. We found that CLCs derived from patients showed crystal packing and Gal10 structure identical to those of Gal10 crystals grown in vitro. When administered to the airways, crystalline Gal10 stimulated innate and adaptive immunity and acted as a type 2 adjuvant. By contrast, a soluble Gal10 mutein was inert. Antibodies directed against key epitopes of the CLC crystallization interface dissolved preexisting CLCs in patient-derived mucus within hours and reversed crystal-driven inflammation, goblet-cell metaplasia, immunoglobulin E (IgE) synthesis, and bronchial hyperreactivity (BHR) in a humanized mouse model of asthma. Thus, protein crystals may promote hallmark features of asthma and are targetable by crystal-dissolving antibodies.


  • Organizational Affiliation

    Immunoregulation Unit, VIB Center for Inflammation Research, Ghent, Belgium.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Galectin-10
A, B, C, D, E
A, B, C, D, E, F
144Homo sapiensMutation(s): 0 
Gene Names: CLCLGALS10LGALS10A
UniProt & NIH Common Fund Data Resources
Find proteins for Q05315 (Homo sapiens)
Explore Q05315 
Go to UniProtKB:  Q05315
PHAROS:  Q05315
GTEx:  ENSG00000105205 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ05315
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
P6G
Query on P6G

Download Ideal Coordinates CCD File 
M [auth E]HEXAETHYLENE GLYCOL
C12 H26 O7
IIRDTKBZINWQAW-UHFFFAOYSA-N
PG4
Query on PG4

Download Ideal Coordinates CCD File 
I [auth B]TETRAETHYLENE GLYCOL
C8 H18 O5
UWHCKJMYHZGTIT-UHFFFAOYSA-N
PGE
Query on PGE

Download Ideal Coordinates CCD File 
G [auth A]
H [auth A]
J [auth B]
K [auth C]
L [auth C]
G [auth A],
H [auth A],
J [auth B],
K [auth C],
L [auth C],
N [auth E],
O [auth F],
P [auth F]
TRIETHYLENE GLYCOL
C6 H14 O4
ZIBGPFATKBEMQZ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.174 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.823α = 90
b = 93.296β = 108.94
c = 93.068γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Belgium--

Revision History  (Full details and data files)

  • Version 1.0: 2019-06-05
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description