Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain

被引：2
|
作者：
Li, Ping [1 ]
Xu, Yuli [1 ]
Li, Xin [1 ]
Bartlam, Mark [1 ]
机构：
[1] Nankai Univ, Coll Life Sci, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
中国国家自然科学基金;
关键词：
casein kinase 2 interacting protein-1; pleckstrin homology (PH) domain; CONTAINING PROTEIN CKIP-1; ACTIN-CAPPING PROTEIN; CELL MORPHOLOGY; KINASE CK2; MEMBRANE; BINDING;
D O I：
10.1107/S1744309113003382
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The casein kinase 2 interacting protein-1 (CKIP-1) is involved in many cellular functions, including apoptosis, signalling pathways, cell growth, cytoskeleton and bone formation. Its N-terminal pleckstrin homology (PH) domain is thought to play an important role in membrane localization and controls shuttling of CKIP-1 between the plasma membrane and nucleus. In this study, the human CKIP-1 PH domain was purified but problems were encountered with nucleic acid contamination. An S84D/S86D/S88D triple mutant designed to abolish nucleic acid binding was purified and successfully crystallized. Single crystals diffracted to 1.7 angstrom resolution and belonged to space group P43212 with unit-cell parameters a = 53.0, b = 53.0, c = 113.8 angstrom, = = = 90.0 degrees.
引用
收藏
页码：324 / 327
页数：4
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