1yyb
From Proteopedia
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| - | [[Image:1yyb.gif|left|200px]] | + | [[Image:1yyb.gif|left|200px]] |
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| - | '''Solution structure of 1-26 fragment of human programmed cell death 5 protein''' | + | {{Structure |
| + | |PDB= 1yyb |SIZE=350|CAPTION= <scene name='initialview01'>1yyb</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of 1-26 fragment of human programmed cell death 5 protein''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YYB is a [ | + | 1YYB is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16083422 16083422] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:59 2008'' |
Revision as of 13:29, 20 March 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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