Dynamic structures of granulocyte colony-stimulating factor proteins studied by normal mode analysis: Two domain-type motions in low frequency modes

Hiromi Sumikawa, Ei Ichiro Suzuki, Ken Ichi Fukuhara, Yasushi Nakajima, Kenshu Kamiya, Hideaki Umeyama

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

In this study, granulocyte colony-stimulating factor (GCSF) proteins were chosen as subjects for normal mode analysis. As helical cytokines with a four helix bundled type topology, they were classified into long chain and short chain groups by Sprang and Bazan. Normal mode calculations were also carried out with leukemia inhibitory factor (LIF), interleukin-6 (IL-6), and growth hormone (GH) as members of the long chain group and GCSF and IL-2 and IL-4 as members of the short chain group. For the GCSF families it was found that the fluctuations in the helical region are smaller than in the loop region, and it is clear that on the whole the smaller fluctuation residues belong to a large hydrophobic core region. Thus, it can be imagined how the receptor binding sites approach the receptor within the normal time-scale of pico seconds. In addition, two similar domain-type motions in low frequency modes were found with proteins in the long chain group, although we never observed any sequence similarity in the two separate two-domain regions in each protein of the long chain group. On the other hand, these two domain- type motions were not clear in proteins of the short chain group.

Original languageEnglish
Pages (from-to)1069-1077
Number of pages9
JournalChemical and Pharmaceutical Bulletin
Volume46
Issue number7
Publication statusPublished - 1998
Externally publishedYes

Keywords

  • Cytokine
  • Granulocyte colony-stimulating factor (GCSF)
  • Interleukin-6 (IL-6)
  • Normal mode analysis

ASJC Scopus subject areas

  • Drug Discovery
  • Organic Chemistry
  • Chemistry(all)
  • Pharmacology

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