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'''Solution structure of 1-26 fragment of human programmed cell death 5 protein'''<br /> | '''Solution structure of 1-26 fragment of human programmed cell death 5 protein'''<br /> | ||
==Overview== | ==Overview== | ||
PDCD5-(1-26) is a N-terminal 26-residue fragment of human PDCD5 | 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. | ||
==About this Structure== | ==About this Structure== | ||
1YYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1YYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Feng, Y | [[Category: Feng, Y G.]] | ||
[[Category: Liu, D | [[Category: Liu, D S.]] | ||
[[Category: Wang, J | [[Category: Wang, J F.]] | ||
[[Category: Yao, H | [[Category: Yao, H W.]] | ||
[[Category: pdcd5(1-26)]] | [[Category: pdcd5(1-26)]] | ||
[[Category: solution structure]] | [[Category: solution structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:22 2008'' | ||
Revision as of 14:10, 21 February 2008
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Solution structure of 1-26 fragment of human programmed cell death 5 protein
Overview
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.
About this Structure
1YYB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character., Liu D, Yao H, Chen Y, Feng Y, Chen Y, Wang J, Biochem J. 2005 Nov 15;392(Pt 1):47-54. PMID:16083422
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