This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1uw5
From Proteopedia
|
STRUCTURE OF PITP-ALPHA COMPLEXED TO PHOSPHATIDYLINOSITOL
Overview
Phosphatidylinositol transfer protein alpha (PITPalpha) selectively, transports and promotes exchange of phosphatidylinositol (PI) and, phosphatidylcholine (PC) between lipid bilayers. In higher eukaryotes, PITPalpha is required for cellular functions such as phospholipase, C-mediated signaling, regulated exocytosis, and secretory vesicle, formation. We have determined the crystal structure of human PITPalpha, bound to its physiological ligand, PI, at 2.95 A resolution. The structure, identifies the critical side chains within the lipid-headgroup binding, pocket that define the exquisite specificity for PI. Mutational analysis, of the PI binding pocket is in good agreement with the structural data and, allows manipulation of functional properties of PITPalpha. Surprisingly, there are no ... [(full description)]
About this Structure
1UW5 is a [Single protein] structure of sequence from [Homo sapiens] with PIE as [ligand]. Structure known Active Site: PI1. Full crystallographic information is available from [OCA].
Reference
Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol., Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ, Structure. 2004 Feb;12(2):317-26. PMID:14962392
Page seeded by OCA on Tue Oct 30 16:12:55 2007
