Molecular Simulation Study on the Interaction between Porcine CR1-like and C3b

The molecular basis of porcine red blood cell immune adhesion function stems from the complement receptor type 1-like (CR1-like) on its cell membrane. The ligand for CR1-like is C3b, which is produced by the cleavage of complement C3; however, the molecular mechanism of the immune adhesion of porcin...

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Published inMolecules (Basel, Switzerland) Vol. 28; no. 5; p. 2183
Main Authors Hou, Zhen, Yin, Wei, Hao, Zhili, Fan, Kuohai, Sun, Na, Sun, Panpan, Li, Hongquan
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 26.02.2023
MDPI
Subjects
Adhesion
Alanine
Alzheimer's disease
Amino acids
Analysis
Animals
Antigens
C3b
Cell membranes
Complement component C3
Complement component C3b
CR1-like
Crystal structure
Erythrocytes
Erythrocytes - metabolism
Homology
immune adhesion
Interaction models
Molecular docking
Molecular Docking Simulation
Molecular dynamics
Molecular structure
Mutation
Optimization
Peptides
Proteins
Receptors, Complement - metabolism
Residues
Simulation
Swine
immune adhesion
CR1-like
C3b
molecular docking
molecular dynamics
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Summary:The molecular basis of porcine red blood cell immune adhesion function stems from the complement receptor type 1-like (CR1-like) on its cell membrane. The ligand for CR1-like is C3b, which is produced by the cleavage of complement C3; however, the molecular mechanism of the immune adhesion of porcine erythrocytes is still unclear. Here, homology modeling was used to construct three-dimensional models of C3b and two fragments of CR1-like. An interaction model of C3b-CR1-like was constructed by molecular docking, and molecular structure optimization was achieved using molecular dynamics simulation. A simulated alanine mutation scan revealed that the amino acids Tyr761, Arg763, Phe765, Thr789, and Val873 of CR1-like SCR 12-14 and the amino acid residues Tyr1210, Asn1244, Val1249, Thr1253, Tyr1267, Val1322, and Val1339 of CR1-like SCR 19-21 are key residues involved in the interaction of porcine C3b with CR1-like. This study investigated the interaction between porcine CR1-like and C3b using molecular simulation to clarify the molecular mechanism of the immune adhesion of porcine erythrocytes.
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ISSN:1420-3049
1420-3049
DOI:10.3390/molecules28052183