Access
To read this story in full you will need to login or make a payment (see right).
News and Views
Nature 456, 337-338 (20 November 2008) | doi:10.1038/456337a; Published online 19 November 2008
Open Innovation Challenges
-
Novel Approaches to Protecting Maize from Insect Damage
The Seeker is looking for novel approaches to protecting maize from insect damage. This Challenge re...
-
Single-cell Analysis Platform
This Challenge is looking for novel approaches to analyzing changes at a single-cell level. This is...
- More Challenges
- Powered by:
nature jobs
Organic Chemistry
- Praj Matrix - Praj Industries Ltd
- Pune, Maharashtra Pune-411021 India
Two Post-Doctoral Position In Nanomedicine
- Fondazione IRCCS Istituto Neurologico "Carlo Besta" (FINCB)
- Via Celoria n.11, 20133 Milano, Italy
Structural biology: Enzyme knocked for a loop
Ronald L. Mellgren1
Abstract
Protein-digesting enzymes are kept on a tight leash to stop them from wantonly attacking targets. Two crystal structures show how an inhibitory protein domain gags one such enzyme without being chewed up itself.
All organisms have enzymes, known as proteinases, that break down other proteins, and have vital roles in such disparate processes as food digestion and blood clotting. These enzymes can't be allowed to run amok — if a protein has been mistakenly broken down, then a replacement has to be painstakingly re-synthesized from scratch.
- Ronald L. Mellgren is in the Department of Physiology and Pharmacology, University of Toledo College of Medicine, Toledo, Ohio 43614-2598, USA.
Email: ronald.mellgren@utoledo.edu
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
How calpain is activated by calciumNature Structural Biology News and Views (01 Apr 2002)
RESEARCH
Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpainsNature Letters to Editor (20 Nov 2008)
Calcium-bound structure of calpain and its mechanism of inhibition by calpastatinNature Letters to Editor (20 Nov 2008)
Crystal structure of calpain reveals the structural basis for Ca 2+ -dependent protease activity and a novel mode of enzyme activationThe EMBO Journal Article (15 Dec 1999)
See all 4 matches for Research