Editor's Summary
9 November 2006
Intramembrane proteolysis
Rhomboid, 
-secretase and related membrane proteins function specifically within the membrane: many signalling proteins undergo intramembrane proteolysis to become activated, and others are converted to poorly soluble and amyloidal peptide fragments. The crystal structure of rhomboid has now been determined, revealing how it utilizes water molecules from outside of the membrane to cleave membrane-embedded protein substrates. This mechanism is likely to be shared by other proteins that catalyse similar reactions. Mutations in one of them, presenilin, are linked to familial Alzheimer's disease.
News and Views: Structural biology: Enzyme theory holds water
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.
Matthew Freeman
doi:10.1038/nature05305
Letter: Structure of C3b reveals conformational changes that underlie complement activity
Bert J. C. Janssen, Agni Christodoulidou, Andrew McCarthy, John D. Lambris and Piet Gros
doi:10.1038/nature05172
First paragraph | Full Text | PDF (762K) | Supplementary information
Letter: Structure of C3b in complex with CRIg gives insights into regulation of complement activation
Christian Wiesmann, Kenneth J. Katschke, JianPing Yin, Karim Y. Helmy, Micah Steffek, Wayne J. Fairbrother, Scott A. McCallum, Lizette Embuscado, Laura DeForge, Philip E. Hass and Menno van Lookeren Campagne
doi:10.1038/nature05263
First paragraph | Full Text | PDF (926K) | Supplementary information
Letter: The structure of complement C3b provides insights into complement activation and regulation
A. Abdul Ajees, K. Gunasekaran, John E. Volanakis, Sthanam. V. L. Narayana, Girish J. Kotwal and H. M. Krishna Murthy
doi:10.1038/nature05258
First paragraph | Full Text | PDF (1,446K) | Supplementary information
