1ICW

INTERLEUKIN-8, MUTANT WITH GLU 38 REPLACED BY CYS AND CYS 50 REPLACED BY ALA

Summary for 1ICW

• Entry DOI: 10.2210/pdb1icw/pdb
• Descriptor: INTERLEUKIN-8 (2 entities in total)
• Functional Keywords: cytokine, chemokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P10145
• Total number of polymer chains: 2
• Total formula weight: 16687.54

Authors

Eigenbrot, C.,Lowman, H.B.,Chee, L.,Artis, D.R. (deposition date: 1996-09-18, release date: 1997-03-12, Last modification date: 2021-11-03)

Primary citation

Eigenbrot, C.,Lowman, H.B.,Chee, L.,Artis, D.R.
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, 27:556-566, 1997

PubMed Abstract: 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.

PubMed: 9141135
DOI: 10.1002/(SICI)1097-0134(199704)27:4<556::AID-PROT8>3.3.CO;2-S

Experimental method

X-RAY DIFFRACTION (2.01 Å)