This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1y32

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR structure of humanin in 30% TFE solution

Structural highlights

1y32 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5]

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Abeta. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6336-41. PMID:11371646 doi:10.1073/pnas.101133498
↑ Ikonen M, Liu B, Hashimoto Y, Ma L, Lee KW, Niikura T, Nishimoto I, Cohen P. Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):13042-7. Epub 2003 Oct 15. PMID:14561895 doi:http://dx.doi.org/10.1073/pnas.2135111100
↑ Hashimoto Y, Niikura T, Ito Y, Sudo H, Hata M, Arakawa E, Abe Y, Kita Y, Nishimoto I. Detailed characterization of neuroprotection by a rescue factor humanin against various Alzheimer's disease-relevant insults. J Neurosci. 2001 Dec 1;21(23):9235-45. PMID:11717357
↑ Guo B, Zhai D, Cabezas E, Welsh K, Nouraini S, Satterthwait AC, Reed JC. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature. 2003 May 22;423(6938):456-61. Epub 2003 May 4. PMID:12732850 doi:http://dx.doi.org/10.1038/nature01627
↑ Ying G, Iribarren P, Zhou Y, Gong W, Zhang N, Yu ZX, Le Y, Cui Y, Wang JM. Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. J Immunol. 2004 Jun 1;172(11):7078-85. PMID:15153530
↑ Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M. Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity. Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:15721287 doi:S0006-291X(05)00120-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==NMR structure of humanin in 30% TFE solution==
-<StructureSection load='1y32' size='340' side='right'caption='[[1y32]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
+<StructureSection load='1y32' size='340' side='right'caption='[[1y32]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. 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>
+<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>
-</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>
+</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>
 </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>
+[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 ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Benaki, D]]
+[[Category: Benaki D]]
-[[Category: Evangelou, A]]
+[[Category: Evangelou A]]
-[[Category: Livaniou, E]]
+[[Category: Livaniou E]]
-[[Category: Mikros, E]]
+[[Category: Mikros E]]
-[[Category: Pelecanou, M]]
+[[Category: Pelecanou M]]
-[[Category: Vlassi, M]]
+[[Category: Vlassi M]]
-[[Category: Zikos, C]]
+[[Category: Zikos C]]
-[[Category: Alzheimer's disease]]
-[[Category: Humanin]]
-[[Category: Neuroprotection]]
-[[Category: Nmr solution structure]]
-[[Category: Unknown function]]

1y32

From Proteopedia

Current revision

NMR structure of humanin in 30% TFE solution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox