Access
To read this story in full you will need to login or make a payment (see right).
News and Views
Nature 444, 153-155 (9 November 2006) | doi:10.1038/nature05305; Published online 11 October 2006
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...
nature jobs
System Engineer (Mechanical)
- Praj Matrix - Praj Industries Ltd
- Pune, Maharashtra Pune-411021 India
Copy Editor
- Indegene Lifesystems Pvt. Ltd
- Bengaluru 560 071 India
Structural biology: Enzyme theory holds water
Matthew Freeman1
Abstract
Intramembrane proteases have attracted much attention because of their biological and medical value. The first crystal structure of one of these enzymes begins to solve the mystery of how they work.
Proteases are some of the most potent tools to which a cell has access, because, unlike most other protein-modifying enzymes, they catalyse an essentially irreversible reaction — the breaking of peptide bonds. This can obviously be used to degrade unwanted proteins, but proteases also have many vital regulatory functions1.
- Matthew Freeman is at the MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Email: mf1@mrc-lmb.cam.ac.uk
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
Structural biology Enzyme theory holds waterNature News and Views
Rhomboid intramembrane protease structures galore!Nature Structural & Molecular Biology News and Views (01 Dec 2006)
RESEARCH
Crystal structure of a rhomboid family intramembrane proteaseNature Article (09 Nov 2006)
Crystal structure of a rhomboid family intramembrane proteaseNature Article
See all 5 matches for Research
