Human programmed cell death 5 protein has a helical-core and two dissociated structural regions.

Abstract

Programmed cell death 5 (PDCD5) protein is phylogenetically conserved in both the nucleus and cytoplasm. The human PDCD5 protein is expressed in tumor cells during apoptosis independent of the apoptosis-inducing stimuli, and recently it was found that PDCD5 is an important regulator in both apoptotic and non-apoptotic programmed cell death. In this study, human PDCD5 was expressed in Escherichia coli cell and studied using heteronuclear NMR method. The NMR results indicate that PDCD5 protein can be divided into three structural regions, a core region and two dissociated terminal regions. The core region (41-101) represents a rigid sub-domain consisting mainly of a triple-helix bundle. The N-terminal 38 residues (3-40) are ordered, but not a rigid structural region which contains abundant secondary structure, and packs very loosely against the core. The C-terminal 17 residues (102-118) represent a mobile unstructured region, which may be capable of interaction with nucleic acid.

• Authors: Dongsheng Liu, Yingang Feng, Yuan Cheng, Jinfeng Wang
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 318 Issue 2 Pg. 391-6 (May 28 2004) ISSN: 0006-291X [Print] United States
• PMID: 15120613 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Apoptosis Regulatory Proteins
• Neoplasm Proteins
• PDCD5 protein, human
• Recombinant Fusion Proteins

Topics

• Amino Acid Sequence
• Amino Acids (chemistry)
• Apoptosis Regulatory Proteins
• Humans
• Hydrophobic and Hydrophilic Interactions
• Molecular Sequence Data
• Neoplasm Proteins (biosynthesis, chemistry, genetics)
• Nuclear Magnetic Resonance, Biomolecular
• Protein Structure, Secondary
• Recombinant Fusion Proteins (biosynthesis, chemistry, genetics)
• Sequence Alignment