Journal home
Advance online publication
Current issue
Archive
Press releases
Supplements
Focus
Guide to authors
Online submissionOnline submission
Permissions
For referees
Free online issue
Contact the journal
Subscribe
Advertising
work@npg
naturereprints
About this site
For librarians
 
NPG Resources
Nature
Nature Cell Biology
Nature Reviews Molecular Cell Biology
The EMBO Journal
Nature Reports Avian Flu
NPG Subject areas
Biotechnology
Cancer
Chemistry
Clinical Medicine
Dentistry
Development
Drug Discovery
Earth Sciences
Evolution & Ecology
Genetics
Immunology
Materials Science
Medical Research
Microbiology
Molecular Cell Biology
Neuroscience
Pharmacology
Physics
Browse all publications
News and Views
Nature Structural Biology  9, 239 - 241 (2002)
doi:10.1038/nsb0402-239

How calpain is activated by calcium

Ahmad Khorchid & Mitsuhiko Ikura

Ahmad Khorchid and Mitsuhiko Ikura are in the Division of Molecular and Structural Biology, Ontario Cancer Institute, and the Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, Canada M5G 2M9.

Correspondence should be addressed to Mitsuhiko Ikura mikura@oci.utoronto.ca
The discovery of two unexpected Ca2+-binding sites in the structure of a minimal catalytic domain of mu-calpain reveals a new mechanism underlying the Ca2+-dependent activation of calpains.

MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated

RESEARCH
Calpain silencing by a reversible intrinsic mechanism
Nature Structural Biology Article (01 May 2003)
Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation
The EMBO Journal Article (15 Dec 1999)

 Top
Abstract
Previous | Next
Table of contents
Full textFull text
Download PDFDownload PDF
Send to a friendSend to a friend
Save this linkSave this link

Open Innovation Challenges

Figures & Tables
Export citation
natureproducts

Search buyers guide:

 
ADVERTISEMENT
 
Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
Journal home | Advance online publication | Current issue | Archive | Press releases | Supplements | For authors | Online submission | Permissions | For referees | Free online issue | About the journal | Contact the journal | Subscribe | Advertising | work@npg | naturereprints | About this site | For librarians
Nature Publishing Group, publisher of Nature, and other science journals and reference works©2002 Nature Publishing Group | Privacy policy