1icw
From Proteopedia
|
INTERLEUKIN-8, MUTANT WITH GLU 38 REPLACED BY CYS AND CYS 50 REPLACED BY ALA
Contents |
Overview
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 binds the three receptors with affinities between 500- and 2,500-fold lower than wild-type IL-8. Binding affinity results are also reported for the variant with alanine substituted for both cysteines 9 and 50. The Glu38-->Cys/Cys50-->Ala IL-8 crystallizes in space group P2(1)2(1)2(1) with cell parameters a = 46.4, b = 49.2, and c = 69.5 A, and has been refined to an R-value of 19.4% for data from 10 to 2 A resolution. Analysis of the structure confirms the new disulfide arrangement and suggests that changes at Ile10 may be the principal cause of the lowered affinities.
Disease
Known disease associated with this structure: AIDS, slow progression to OMIM:[146929]
About this Structure
1ICW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural change and receptor binding in a chemokine mutant with a rearranged disulfide: X-ray structure of E38C/C50AIL-8 at 2 A resolution., Eigenbrot C, Lowman HB, Chee L, Artis DR, Proteins. 1997 Apr;27(4):556-66. PMID:9141135
Page seeded by OCA on Thu Feb 21 13:10:30 2008
