A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.
Collagen
/ chemistry
Complement Activation
Mannose-Binding Lectin
/ chemistry
Solutions
/ chemistry
Protein Conformation
Peptide Fragments
/ chemistry
Structure-Activity Relationship
Protein Stability
Scattering, Small Angle
Neutron Diffraction
Ultracentrifugation
Molecular Dynamics Simulation
Crystallography, X-Ray
Pliability
analytical ultracentrifugation
atomistic modeling
collagen
complement
molecular dynamics
small-angle X-ray scattering
small-angle neutron scattering
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
received:
03
04
2022
revised:
05
12
2022
accepted:
09
12
2022
pubmed:
18
12
2022
medline:
25
2
2023
entrez:
17
12
2022
Statut:
ppublish
Résumé
Collagen triple helices are critical in the function of mannan-binding lectin (MBL), an oligomeric recognition molecule in complement activation. The MBL collagen regions form complexes with the serine proteases MASP-1 and MASP-2 in order to activate complement, and mutations lead to common immunodeficiencies. To evaluate their structure-function properties, we studied the solution structures of four MBL-like collagen peptides. The thermal stability of the MBL collagen region was much reduced by the presence of a GQG interruption in the typical (X-Y-Gly)n repeat compared to controls. Experimental solution structural data were collected using analytical ultracentrifugation and small angle X-ray and neutron scattering. As controls, we included two standard Pro-Hyp-Gly collagen peptides (POG)
Identifiants
pubmed: 36528062
pii: S0021-9258(22)01242-X
doi: 10.1016/j.jbc.2022.102799
pmc: PMC9898670
pii:
doi:
Substances chimiques
Collagen
9007-34-5
Mannose-Binding Lectin
0
Solutions
0
Peptide Fragments
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
102799Subventions
Organisme : Medical Research Council
ID : MR/K011715/1
Pays : United Kingdom
Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.