Crystal structure of the tyrosine kinase domain of the human insulin receptor

Stevan R. Hubbard, Lei Wei, Wayne A. Hendrickson

Research output: Contribution to journalArticle

877 Citations (Scopus)

Abstract

The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 Å resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.

Original languageEnglish (US)
Pages (from-to)746-754
Number of pages9
JournalNature
Volume372
Issue number6508
StatePublished - 1994
Externally publishedYes

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Protein-Tyrosine Kinases
Tyrosine
Threonine
Serine
Catalytic Domain
X-Rays
Insulin
human INSR protein

ASJC Scopus subject areas

  • Medicine(all)
  • General

Cite this

Hubbard, S. R., Wei, L., & Hendrickson, W. A. (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature, 372(6508), 746-754.

Crystal structure of the tyrosine kinase domain of the human insulin receptor. / Hubbard, Stevan R.; Wei, Lei; Hendrickson, Wayne A.

In: Nature, Vol. 372, No. 6508, 1994, p. 746-754.

Research output: Contribution to journalArticle

Hubbard, SR, Wei, L & Hendrickson, WA 1994, 'Crystal structure of the tyrosine kinase domain of the human insulin receptor', Nature, vol. 372, no. 6508, pp. 746-754.
Hubbard, Stevan R. ; Wei, Lei ; Hendrickson, Wayne A. / Crystal structure of the tyrosine kinase domain of the human insulin receptor. In: Nature. 1994 ; Vol. 372, No. 6508. pp. 746-754.
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