Cryo-EM of the human insulin receptor ectodomain in complex with an insulin analog with truncated B chain and enlongated A chain
Ontology highlight
ABSTRACT:
SUBMITTER: Alan D Blakely
PROVIDER: EMPIAR-10736 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Symmetric and asymmetric receptor conformation continuum induced by a new insulin.
Xiong Xiaochun X Blakely Alan A Kim Jin Hwan JH Menting John G JG Schäfer Ingmar B IB Schubert Heidi L HL Agrawal Rahul R Gutmann Theresia T Delaine Carlie C Zhang Yi Wolf YW Artik Gizem Olay GO Merriman Allanah A Eckert Debbie D Lawrence Michael C MC Coskun Ünal Ü Fisher Simon J SJ Forbes Briony E BE Safavi-Hemami Helena H Hill Christopher P CP Chou Danny Hung-Chieh DH
Nature chemical biology 20220314 5
Cone snail venoms contain a wide variety of bioactive peptides, including insulin-like molecules with distinct structural features, binding modes and biochemical properties. Here, we report an active humanized cone snail venom insulin with an elongated A chain and a truncated B chain, and use cryo-electron microscopy (cryo-EM) and protein engineering to elucidate its interactions with the human insulin receptor (IR) ectodomain. We reveal how an extended A chain can compensate for deletion of B-c ...[more]
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