1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8

Krishnakumar Rajarathnam, Ian Clark-Lewis, Beatrice Dewald, Marco Baggiolini, Brian D. Sykes

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


In order to assess the importance of the buried Glu-38 observed in the structure of interleukin-8, an analog in which Glu-38 was replaced with Ala (E38A analog) was investigated by 1H NMR spectroscopy and neutrophil activation. Detailed analysis of the NMR NOESY data showed that the solution structure of the E38A analog is essentially the same as that for the native protein. Also, the neutrophil elastase activity of the E38A analog was similar to that of the native protein. However, the Gln-8 and Cys-9 amide proton chemical shifts, which are significantly downfield-shifted in the native protein, exhibit more 'normal' values. This observation indicates that in the native protein, Glu-38 side-chain carboxylate interacts with Gln-8 and Cys-9 amide protons. Although the N-terminal residues are critical for function, this interaction is not essential for neutrophil activation.

Original languageEnglish (US)
Pages (from-to)43-46
Number of pages4
JournalFEBS Letters
Issue number1-2
StatePublished - Dec 9 1996
Externally publishedYes


  • Chemokine
  • H-bonding interaction
  • Interleukin-8
  • NMR
  • Structure-function

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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