Homology model for oncostatin M based on NMR structural data

Douglas Kitchen, Ross C. Huffman, Franklin J. Moy, Robert Powers

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Oncostatin M (OM) is a member of the cytokine family which regulates the proliferation and differentiation of a variety of cell types and includes interleukin-6 (IL-6), leukemia inhibitory factor (LIF), and granulocyte- colony stimulating factor (G-CSF). This family of proteins adopts a four- helix bundle fold with up-up-down-down topology and contains intramolecular disulfide bonds. Since an X-ray or NMR structure for OM is not currently available, a homology model for OM was determined from the X-ray structures of human growth hormone (hGH), LIF, and G-CSF where the alignment was based on secondary structure instead of sequence. The OM secondary structure was determined from NMR structural data, and the secondary structures for hGH, LIF, and G-CSF were obtained from the reported X-ray structures. The resulting homology model was refined using sequential NOE distance 13C restraints, chemical shift information, and a conformational database.

Original languageEnglish (US)
Pages (from-to)10581-10588
Number of pages8
JournalBiochemistry
Volume37
Issue number30
DOIs
StatePublished - Jul 28 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Homology model for oncostatin M based on NMR structural data'. Together they form a unique fingerprint.

Cite this