2ETT

Solution Structure of Human Sorting Nexin 22 PX Domain

2ETT の概要

• エントリーDOI: 10.2210/pdb2ett/pdb
• 分子名称: Sorting nexin-22 (1 entity in total)
• 機能のキーワード: px domain, sorting nexin 22, bc019655, snx22_human, hs.157607, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q96L94
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15219.48

構造登録者

Song, J.,Zhao, Q.,Tyler, R.C.,Lee, M.S.,Newman, C.L.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2005-10-27, 公開日: 2005-11-15, 最終更新日: 2024-05-22)

主引用文献

Song, J.,Zhao, K.Q.,Newman, C.L.,Vinarov, D.A.,Markley, J.L.
Solution structure of human sorting nexin 22.
Protein Sci., 16:807-814, 2007

PubMed Abstract: 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.

PubMed: 17400918
DOI: 10.1110/ps.072752407

実験手法

SOLUTION NMR