Structural basis of IAP recognition by Smac/DIABLO View Full Text


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Article Info

DATE

2000-12

AUTHORS

Geng Wu, Jijie Chai, Tomeka L. Suber, Jia-Wei Wu, Chunying Du, Xiaodong Wang, Yigong Shi

ABSTRACT

Apoptosis is an essential process in the development and homeostasis of all metazoans. The inhibitor-of-apoptosis (IAP) proteins suppress cell death by inhibiting the activity of caspases; this inhibition is performed by the zinc-binding BIR domains of the IAP proteins. The mitochondrial protein Smac/DIABLO promotes apoptosis by eliminating the inhibitory effect of IAPs through physical interactions. Amino-terminal sequences in Smac/DIABLO are required for this function, as mutation of the very first amino acid leads to loss of interaction with IAPs and concomitant loss of Smac/DIABLO function. Here we report the high-resolution crystal structure of Smac/DIABLO complexed with the third BIR domain (BIR3) of XIAP. Our results show that the N-terminal four residues (Ala-Val-Pro-Ile) in Smac/DIABLO recognize a surface groove on BIR3, with the first residue Ala binding a hydrophobic pocket and making five hydrogen bonds to neighbouring residues on BIR3. These observations provide a structural explanation for the roles of the Smac N terminus as well as the conserved N-terminal sequences in the Drosophila proteins Hid/Grim/Reaper. In conjunction with other observations, our results reveal how Smac may relieve IAP inhibition of caspase-9 activity. In addition to explaining a number of biological observations, our structural analysis identifies potential targets for drug screening. More... »

PAGES

1008

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6815

VOLUME

408

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35050012

    DOI

    http://dx.doi.org/10.1038/35050012

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1013741960

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11140638


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