2jbu

From Proteopedia

Revision as of 15:24, 30 October 2007

CRYSTAL STRUCTURE OF HUMAN INSULIN DEGRADING ENZYME COMPLEXED WITH CO-PURIFIED PEPTIDES.

Overview

Insulin-degrading enzyme (IDE) is a zinc metalloprotease that hydrolyzes, amyloid-beta (Abeta) and insulin, which are peptides associated with, Alzheimer disease (AD) and diabetes, respectively. Our previous structural, analysis of substrate-bound human 113-kDa IDE reveals that the N- and, C-terminal domains of IDE, IDE-N and IDE-C, make substantial contact to, form an enclosed catalytic chamber to entrap its substrates. Furthermore, IDE undergoes a switch between the closed and open conformations for, catalysis. Here we report a substrate-free IDE structure in its closed, conformation, revealing the molecular details of the active conformation, of the catalytic site of IDE and new insights as to how the closed, conformation of IDE may be kept in its resting, inactive conformation. We, ... [(full description)]

About this Structure

2JBU is a [Single protein] structure of sequence from [Escherichia coli] and [Homo sapiens] with DIO as [ligand]. Active as [Insulysin], with EC number [3.4.24.56]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of Substrate-free Human Insulin-degrading Enzyme (IDE) and Biophysical Analysis of ATP-induced Conformational Switch of IDE., Im H, Manolopoulou M, Malito E, Shen Y, Zhao J, Neant-Fery M, Sun CY, Meredith SC, Sisodia SS, Leissring MA, Tang WJ, J Biol Chem. 2007 Aug 31;282(35):25453-63. Epub 2007 Jul 5. PMID:17613531

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