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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 69; no. 3; pp. 324 - 327
• Main Authors: Li, Ping, Xu, Yuli, Li, Xin, Bartlam, Mark
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.03.2013
• Subjects: Amino Acid Substitution; Aspartic Acid - chemistry; Aspartic Acid - genetics; Carrier Proteins - chemistry; Carrier Proteins - genetics; casein kinase 2 interacting protein-1; Crystallization; Crystallization Communications; Crystallography; Crystallography, X-Ray; Escherichia coli - chemistry; Escherichia coli - genetics; Homology; Human; Humans; Intracellular Signaling Peptides and Proteins; Kinases; Membranes; Mutation; Nucleic acids; Nucleic Acids - chemistry; pleckstrin homology (PH) domain; Protein Structure, Tertiary; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Serine - chemistry; Serine - genetics; pleckstrin homology (PH) domain; casein kinase 2 interacting protein-1
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309113003382

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 Å resolution and belonged to space group P43212 with unit‐cell parameters a = 53.0, b = 53.0, c = 113.8 Å, α = β = γ = 90.0°.