Solution structure of human insulin-like growth factor II; Recognition sites for receptors and binding proteins

Hiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Koji Nagata, Nobuyuki Higashihashi, Hiroyuki Fujiwara, Katsu Ichi Sakano, Fuyuhiko Inagaki

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The three-dimensional structure of human insulin-like growth factor II was determined at high resolution in aqueous solution by NMR and simulated annealing based calculations. The structure is quite similar to those of insulin and insulin-like growth factor I, which consists of an α-helix followed by a turn and a strand in the B-region and two antiparallel α-helices in the A-region. However, the regions of Ala1-Glu6, Pro31-Arg40 and Thr62-Glu67 are not well-defined for lack of distance constraints, possibly due to motional flexibility. Based on the resultant structure and the results of structure-activity relationships, we propose the interaction sites of insulin-like growth factor II with the type 2 insulin-like growth factor receptor and the insulin-like growth factor binding proteins. These sites partially overlap with each other at the opposite side of the putative binding surface to the insulin receptor and the type 1 insulin-like growth factor receptor. We also discuss the interaction modes of insulin-like growth factor II with the insulin receptor and the type 1 insulin-like growth factor receptor.

Original languageEnglish
Pages (from-to)5590-5597
Number of pages8
JournalEMBO Journal
Volume13
Issue number23
DOIs
Publication statusPublished - Dec 1 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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