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TitleThe signalling conformation of the insulin receptor ectodomain.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 4420, Year 2018
Publish dateOct 24, 2018
AuthorsFelix Weis / John G Menting / Mai B Margetts / Shu Jin Chan / Yibin Xu / Norbert Tennagels / Paulus Wohlfart / Thomas Langer / Christoph W Müller / Matthias K Dreyer / Michael C Lawrence /
PubMed AbstractUnderstanding the structural biology of the insulin receptor and how it signals is of key importance in the development of insulin analogs to treat diabetes. We report here a cryo-electron microscopy ...Understanding the structural biology of the insulin receptor and how it signals is of key importance in the development of insulin analogs to treat diabetes. We report here a cryo-electron microscopy structure of a single insulin bound to a physiologically relevant, high-affinity version of the receptor ectodomain, the latter generated through attachment of C-terminal leucine zipper elements to overcome the conformational flexibility associated with ectodomain truncation. The resolution of the cryo-electron microscopy maps is 3.2 Å in the insulin-binding region and 4.2 Å in the membrane-proximal region. The structure reveals how the membrane proximal domains of the receptor come together to effect signalling and how insulin's negative cooperativity of binding likely arises. Our structure further provides insight into the high affinity of certain super-mitogenic insulins. Together, these findings provide a new platform for insulin analog investigation and design.
External linksNat Commun / PubMed:30356040 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.2 Å
Structure data

0246

6hn4

EMDB-0246, PDB-6hn4:
Leucine-zippered human insulin receptor ectodomain with single bound insulin - "lower" membrane-proximal part
Method: EM (single particle) / Resolution: 4.2 Å

0247

6hn5

EMDB-0247, PDB-6hn5:
Leucine-zippered human insulin receptor ectodomain with single bound insulin - "upper" membrane-distal part
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsSIGNALING PROTEIN / insulin / insulin receptor ectodomain / signal transdution / signal transduction

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