Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1
Version of Record online: 20 APR 2013
Copyright © 2013 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 81, Issue 7, pages 1266–1270, July 2013
How to Cite
Jin, T., Curry, J., Smith, P., Jiang, J. and Xiao, T. S. (2013), Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1. Proteins, 81: 1266–1270. doi: 10.1002/prot.24287
- Issue online: 17 JUN 2013
- Version of Record online: 20 APR 2013
- Accepted manuscript online: 18 MAR 2013 10:44AM EST
- Manuscript Accepted: 2 MAR 2013
- Manuscript Revised: 26 FEB 2013
- Manuscript Received: 18 DEC 2012
- National Cancer Institute . Grant Number: Y1-CO-1020
- National Institute of General Medical Sciences . Grant Number: Y1-GM-1104
- US Department of Energy . Grant Number: DE-AC02-06CH11357
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases, NIH
Additional Supporting Information may be found in the online version of this article.
Supplemental Figure 1. Electron density map (2Fo-Fc) contoured at 1.0 sigma near the α4-α5 loop is shown as blue mesh for 4IFP (A) and 3KAT (B). C. The α6 helix of the MBP-NLRP1-CARD are involved in crystal lattice contacts with residue W1460 binding its symmetry mate. The NLRP1 CARD is colored magenta and pink, and the W1460 residues are shown as sticks and marked. D. A similar view of the 3KAT α6 helix is shown in yellow and wheat.
Table S1. Comparison of the MBP-NLRP1 CARD (4IFP) and NLRP1 CARD (3KAT) crystal structures using the Molprobity server and the Phenix program
Table S2. Comparison of the NLRP1 CARD structure (4IFP) with other CARD structures by the Dali server (http://ekhidna.biocenter.helsinki.fi/dali_server/start)
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