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 in | Molecules (Basel, Switzerland) Vol. 28; no. 5; p. 2183 |
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Main Authors | , , , , , , |
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Abstract | 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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AbstractList | 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. |
Audience | Academic |
Author | Hou, Zhen Hao, Zhili Sun, Panpan Li, Hongquan Fan, Kuohai Sun, Na Yin, Wei |
AuthorAffiliation | 1 Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China 2 College of Veterinary Medicine, Jilin University, Changchun 130015, China |
AuthorAffiliation_xml | – name: 1 Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – name: 2 College of Veterinary Medicine, Jilin University, Changchun 130015, China |
Author_xml | – sequence: 1 givenname: Zhen orcidid: 0000-0002-5476-1441 surname: Hou fullname: Hou, Zhen organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – sequence: 2 givenname: Wei surname: Yin fullname: Yin, Wei organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – sequence: 3 givenname: Zhili surname: Hao fullname: Hao, Zhili organization: College of Veterinary Medicine, Jilin University, Changchun 130015, China – sequence: 4 givenname: Kuohai surname: Fan fullname: Fan, Kuohai organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – sequence: 5 givenname: Na surname: Sun fullname: Sun, Na organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – sequence: 6 givenname: Panpan surname: Sun fullname: Sun, Panpan organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China – sequence: 7 givenname: Hongquan surname: Li fullname: Li, Hongquan organization: Shanxi Key Lab for Modernization of TCVM, College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China |
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SubjectTerms | 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 |
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Title | Molecular Simulation Study on the Interaction between Porcine CR1-like and C3b |
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