2ett

From Proteopedia

Revision as of 11:55, 23 January 2008

Solution Structure of Human Sorting Nexin 22 PX Domain

Overview

The sorting nexins (SNXs) constitute a large group of PX domain-containing, proteins that play critical roles in protein trafficking. We report here, the solution structure of human sorting nexin 22 (SNX22). Although SNX22, has <30% sequence identity with any PX domain protein of known structure, it was found to contain the alpha/beta fold and compact structural core, characteristic of PX domains. Analysis of the backbone dynamics of SNX22, by NMR relaxation measurements revealed that the two walls of the ligand, binding cleft undergo internal motions: on the picosecond timescale for, the beta1/beta2 loop and on the micro- to millisecond timescale for the, loop between the polyproline motif and helix alpha2. Regions of the SNX22, structure that differ from those of other PX domains include the loop, connecting strands beta1 and beta2 and the loop connecting helices alpha1, and alpha2, which appear to be more mobile than corresponding loops in, other known structures. The interaction of, dibutanoyl-phosphatidylinositol-3-phosphate (dibutanoyl-PtdIns(3)P) with, SNX22 was investigated by an NMR titration experiment, which identified, the binding site in a basic cleft and indicated that ligand binding leads, only to a local structural rearrangement as has been found with other PX, domains. Because motions in the loops are damped out when, dibutanoyl-PtdIns(3)P binds, entropic effects could contribute to the, lower affinity of SNX22 for this ligand compared to other PX domains.

About this Structure

2ETT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of human sorting nexin 22., Song J, Zhao KQ, Newman CL, Vinarov DA, Markley JL, Protein Sci. 2007 May;16(5):807-14. Epub 2007 Mar 30. PMID:17400918

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