The crystal structure of GXGD membrane protease FlaK

Jian Hu, Yi Xue, Sangwon Lee and Ya Ha ()
Additional contact information
Jian Hu: Yale School of Medicine
Yi Xue: Yale School of Medicine
Sangwon Lee: Yale School of Medicine
Ya Ha: Yale School of Medicine

Nature, 2011, vol. 475, issue 7357, 528-531

Abstract: Membrane aspartyl protease structure The GXGD family of intramembrane proteases includes presenilin, which is mutated in familial Alzheimer's disease, and type 4 prepilin peptidases, which are virulence factors for many pathogenic bacteria. The first crystal structure of a GXGD membrane protease has now been determined. The structure of the FlaK preflagellin peptidase from Methanococcus maripaludis reveals fundamental differences between the GXGD membrane aspartyl protease and its soluble counterparts such as pepsin. Comparison with models of presenilin derived from biochemical analysis suggests that the structure of its active site is similar to that of archaeal FlaK. This structural knowledge will facilitate rational design of inhibitors that target this family of proteases.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature10218 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:475:y:2011:i:7357:d:10.1038_nature10218

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature10218

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().