1y32

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:30, 6 December 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1y32.png|left|200px]]
 
-
<!--
+
==NMR structure of humanin in 30% TFE solution==
-
The line below this paragraph, containing "STRUCTURE_1y32", creates the "Structure Box" on the page.
+
<StructureSection load='1y32' size='340' side='right'caption='[[1y32]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1y32]] 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=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [https://pdbe.org/1y32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [https://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>
-
{{STRUCTURE_1y32| PDB=1y32 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Humanin is a newly identified 24-residue peptide that suppresses neuronal cell death caused by a wide spectrum of familial Alzheimer's disease genes and the beta-amyloid peptide. In this study, NMR and circular dichroism studies of synthetic humanin in aqueous and 30% 2,2,2-trifluoroethanol (TFE) solutions are reported. In aqueous solution, humanin exists predominantly in an unstructured conformation in equilibrium with turn-like structures involving residues Gly5 to Leu10 and Glu15 to Leu18, providing indication of nascent helix. In the less polar environment of 30% TFE, humanin readily adopts helical structure with long-range order spanning residues Gly5 to Leu18. Comparative 3D modeling studies and topology predictions are in qualitative agreement with the experimental findings in both environments. Our studies reveal a flexible peptide in aqueous environment, which is free to interact with possible receptors that mediate its action, but may also acquire a helical conformation necessary for specific interactions and/or passage through membranes.
-
===NMR structure of humanin in 30% TFE solution===
+
Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity.,Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:15721287<ref>PMID:15721287</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_15721287}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1y32" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 15721287 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15721287}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Homo sapiens]]
-
1Y32 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Benaki D]]
-
==Reference==
+
[[Category: Evangelou A]]
-
Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity., Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M, Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15721287 15721287]
+
[[Category: Livaniou E]]
-
[[Category: Single protein]]
+
[[Category: Mikros E]]
-
[[Category: Benaki, D.]]
+
[[Category: Pelecanou M]]
-
[[Category: Evangelou, A.]]
+
[[Category: Vlassi M]]
-
[[Category: Livaniou, E.]]
+
[[Category: Zikos C]]
-
[[Category: Mikros, E.]]
+
-
[[Category: Pelecanou, M.]]
+
-
[[Category: Vlassi, M.]]
+
-
[[Category: Zikos, C.]]
+
-
[[Category: Alzheimer's disease]]
+
-
[[Category: Humanin]]
+
-
[[Category: Neuroprotection]]
+
-
[[Category: Nmr solution structure]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:42:04 2008''
+

Current revision

NMR structure of humanin in 30% TFE solution

PDB ID 1y32

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y32"
Personal tools