Article
Structural change and receptor binding in a chemokine mutant with a rearranged disulfide: X-ray structure of E38C/C50AIL-8 at 2 A resolution.
Proteins - 1 Apr 1997
Eigenbrot C, Lowman H B, Chee L, Artis D R
Abstract excerpt
The characteristic CXC chemokine disulfide core of interleukin-8 (IL-8) has been rearranged in a variant replacing the 9-50 disulfide with a 9-38 disulfide. The new variant has been characterized by its binding affinity to IL-8 receptors A and B and the erythrocyte receptor DARC. This variant bin...
Topics
- Antigens, CD
- Binding Sites
- Binding, Competitive
- Computer Simulation
- Crystallography, X-Ray
- Cysteine
- Disulfides
- Erythrocytes
- Interleukin-8
- Models, Molecular
- Mutation
- Neutrophils
- Protein Conformation
- Receptors, Interleukin
- Receptors, Interleukin-8A
- Water