Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
Binding Sites
Complement C3-C5 Convertases
/ chemistry
Complement System Proteins
/ chemistry
HEK293 Cells
Humans
Models, Molecular
Mutation
Properdin
/ chemistry
Protein Binding
Protein Conformation
Protein Multimerization
Protein Processing, Post-Translational
Proteolysis
Structure-Activity Relationship
complement
complement component C3
convertase
crystal structure
factor B
properdin
regulation
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2019
2019
Historique:
received:
21
06
2019
accepted:
07
08
2019
entrez:
12
9
2019
pubmed:
12
9
2019
medline:
2
10
2020
Statut:
epublish
Résumé
Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system. Here we present two crystal structures of FP and two structures of convertase bound FP. A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b. Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg
Identifiants
pubmed: 31507604
doi: 10.3389/fimmu.2019.02007
pmc: PMC6713926
doi:
Substances chimiques
Properdin
11016-39-0
Complement System Proteins
9007-36-7
Complement C3-C5 Convertases
EC 3.4.21.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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