Characterization of single amino acid substitutions in the β2 integrin subunit of patients with leukocyte adhesion deficiency (LAD)-1
| Autor: | Gulbu Uzel, Siyu Guan, S. K. Alex Law, Suet-Mien Tan, Yan Li, Jaume Torres, Liming Xiang |
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| Přispěvatelé: | School of Biological Sciences, School of Physical and Mathematical Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Leukocyte-Adhesion Deficiency Syndrome Molecular Sequence Data Integrin Mutation Missense Gene Expression CD18 Science::Biological sciences::Molecular biology [DRNTU] Biology Transfection medicine.disease_cause Protein Structure Secondary Cell Adhesion Leukocytes medicine Humans Missense mutation Amino Acid Sequence Cell adhesion Molecular Biology Leukocyte adhesion deficiency Mutation Leukocyte adhesion deficiency-1 Cell Biology Hematology medicine.disease Molecular biology Recombinant Proteins Protein Structure Tertiary Protein Subunits HEK293 Cells Amino Acid Substitution Integrin alpha M CD18 Antigens biology.protein Molecular Medicine Sequence Alignment Plasmids |
| Popis: | Leukocyte adhesion deficiency 1 (LAD-1) is caused by defects in the β2 integrin subunit. We studied 18 missense mutations, 14 of which fail to support the surface expression of the β2 integrins. Integrins with the β2-G150D mutation fail to bind ligands, possibly due to the failure of the α1 segment of the βI domain to assume an α-helical structure. Integrins with the β2-G716A mutation are not maintained in their resting states, and the patient has the severe phenotype of LAD-1. The β2-S453N and β2-P648L mutants support the expression of integrins and adhesion functions. They should be re-classified as polymorphic variants. Accepted version |
| Databáze: | OpenAIRE |
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