Literature DB >> 11257230

Structural basis of caspase-7 inhibition by XIAP.

J Chai1, E Shiozaki, S M Srinivasula, Q Wu, P Datta, E S Alnemri, Y Shi, P Dataa.   

Abstract

The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.

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Year:  2001        PMID: 11257230     DOI: 10.1016/s0092-8674(01)00272-0

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  162 in total

1.  Oligomerization and activation of caspase-9, induced by Apaf-1 CARD.

Authors:  Eric N Shiozaki; Jijie Chai; Yigong Shi
Journal:  Proc Natl Acad Sci U S A       Date:  2002-03-19       Impact factor: 11.205

2.  A novel role for XIAP in copper homeostasis through regulation of MURR1.

Authors:  Ezra Burstein; Lakshmanan Ganesh; Robert D Dick; Bart van De Sluis; John C Wilkinson; Leo W J Klomp; Cisca Wijmenga; George J Brewer; Gary J Nabel; Colin S Duckett
Journal:  EMBO J       Date:  2003-12-18       Impact factor: 11.598

Review 3.  Caspase activation, inhibition, and reactivation: a mechanistic view.

Authors:  Yigong Shi
Journal:  Protein Sci       Date:  2004-08       Impact factor: 6.725

Review 4.  The protein structures that shape caspase activity, specificity, activation and inhibition.

Authors:  Pablo Fuentes-Prior; Guy S Salvesen
Journal:  Biochem J       Date:  2004-12-01       Impact factor: 3.857

Review 5.  Mechanisms of cell death in heart disease.

Authors:  Klitos Konstantinidis; Russell S Whelan; Richard N Kitsis
Journal:  Arterioscler Thromb Vasc Biol       Date:  2012-05-17       Impact factor: 8.311

6.  Lipid-conjugated Smac analogues.

Authors:  Ewa D Micewicz; Josephine A Ratikan; Alan J Waring; Julian P Whitelegge; William H McBride; Piotr Ruchala
Journal:  Bioorg Med Chem Lett       Date:  2015-09-08       Impact factor: 2.823

7.  The BIR domain of IAP-like protein 2 is conformationally unstable: implications for caspase inhibition.

Authors:  Hwain Shin; Martin Renatus; Brendan P Eckelman; Viviane A Nunes; Claudio A M Sampaio; Guy S Salvesen
Journal:  Biochem J       Date:  2005-01-01       Impact factor: 3.857

8.  Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP.

Authors:  Domagoj Vucic; Matthew C Franklin; Heidi J A Wallweber; Kanad Das; Brendan P Eckelman; Hwain Shin; Linda O Elliott; Saloumeh Kadkhodayan; Kurt Deshayes; Guy S Salvesen; Wayne J Fairbrother
Journal:  Biochem J       Date:  2005-01-01       Impact factor: 3.857

9.  Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.

Authors:  Brett Feeney; Cristina Pop; Paul Swartz; Carla Mattos; A Clay Clark
Journal:  Biochemistry       Date:  2006-11-07       Impact factor: 3.162

10.  Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector.

Authors:  Ana C Figueiredo; Daniele de Sanctis; Ricardo Gutiérrez-Gallego; Tatiana B Cereija; Sandra Macedo-Ribeiro; Pablo Fuentes-Prior; Pedro José Barbosa Pereira
Journal:  Proc Natl Acad Sci U S A       Date:  2012-12-05       Impact factor: 11.205

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