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[[Image:1yyb.gif|left|200px]]
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{{STRUCTURE_1yyb|  PDB=1yyb  |  SCENE=  }}
'''Solution structure of 1-26 fragment of human programmed cell death 5 protein'''


==Solution structure of 1-26 fragment of human programmed cell death 5 protein==
<StructureSection load='1yyb' size='340' side='right'caption='[[1yyb]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yyb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YYB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyb OCA], [https://pdbe.org/1yyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yyb RCSB], [https://www.ebi.ac.uk/pdbsum/1yyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDCD5_HUMAN PDCD5_HUMAN] May function in the process of apoptosis.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16083422</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1yyb" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Cell death protein 3D structures|Cell death protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Feng, Y G.]]
[[Category: Feng YG]]
[[Category: Liu, D S.]]
[[Category: Liu DS]]
[[Category: Wang, J F.]]
[[Category: Wang JF]]
[[Category: Yao, H W.]]
[[Category: Yao HW]]
[[Category: Solution structure]]
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Retrieved from "https://proteopedia.org/1yyb"