1YYB

Solution structure of 1-26 fragment of human programmed cell death 5 protein

Summary for 1YYB

• Entry DOI: 10.2210/pdb1yyb/pdb
• NMR Information: BMRB: 6556
• Descriptor: Programmed cell death protein 5 (1 entity in total)
• Functional Keywords: pdcd5(1-26), solution structure, apoptosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 2967.19

Authors

Liu, D.S.,Feng, Y.G.,Yao, H.W.,Wang, J.F. (deposition date: 2005-02-24, release date: 2005-09-13, Last modification date: 2024-05-29)

Primary citation

Liu, D.,Yao, H.,Chen, Y.,Feng, Y.,Chen, Y.,Wang, J.
The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character.
Biochem.J., 392:47-54, 2005

PubMed Abstract: PDCD5-(1-26) is a N-terminal 26-residue fragment of human PDCD5 (programmed cell death 5) protein. PDCD5 is an important novel protein that regulates both apoptotic and non-apoptotic programmed cell death. The conformation of PDCD5 protein is a stable helical core consisting of a triple-helix bundle and two dissociated terminal regions. The N-terminal region is ordered and contains abundant secondary structure. Overexpression and purification of the N-terminal 26-residure fragment, PDCD5-(1-26), was performed in this study to better understand its tertiary structure. The spectroscopic studies using CD and hetero- and homo-nuclear NMR methods determine a stable alpha-helix formed by Asp3-Ala19 of PDCD5-(1-26). The N-terminal residues Asp3-Ala19 of PDCD5 were then affirmed to have the capacity to form a stable alpha-helix independently of the core of the protein. Analysis of the helical peptide of PDCD5-(1-26) indicates that the surface of this well-formed alpha-helix has a unique electrostatic potential character. This may provide an environment for the N-terminal alpha-helix of PDCD5 to serve as an independent functional entity of the protein. The apoptosis activity assay shows that the deletion of the N-terminal alpha-helix of PDCD5 significantly attenuates the apoptosis-promoting effects on HL-60 cells induced by serum withdrawal.

PubMed: 16083422
DOI: 10.1042/BJ20050688

Experimental method

SOLUTION NMR