2yt0

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{{Seed}}
 
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[[Image:2yt0.png|left|200px]]
 
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==Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L==
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The line below this paragraph, containing "STRUCTURE_2yt0", creates the "Structure Box" on the page.
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<StructureSection load='2yt0' size='340' side='right'caption='[[2yt0]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2yt0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YT0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yt0 OCA], [https://pdbe.org/2yt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yt0 RCSB], [https://www.ebi.ac.uk/pdbsum/2yt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yt0 ProSAT], [https://www.topsan.org/Proteins/RSGI/2yt0 TOPSAN]</span></td></tr>
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{{STRUCTURE_2yt0| PDB=2yt0 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APBB2_MOUSE APBB2_MOUSE] May modulate the internalization of beta-amyloid precursor protein (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yt/2yt0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2yt0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fe65L1, a member of the Fe65 family, is an adaptor protein that interacts with the cytoplasmic domain of Alzheimer amyloid precursor protein (APP) through its C-terminal phosphotyrosine interaction/phosphotyrosine binding (PID/PTB) domain. In the present study, the solution structures of the C-terminal PID domain of mouse Fe65L1, alone and in complex with a 32-mer peptide (DAAVTPEERHLSKMQQNGYENPTYKFFEQMQN) derived from the cytoplasmic domain of APP, were determined using NMR spectroscopy. The C-terminal PID domain of Fe65L1 alone exhibits a canonical PID/PTB fold, whereas the complex structure reveals a novel mode of peptide binding. In the complex structure, the NPTY motif forms a type-I beta-turn, and the residues immediately N-terminal to the NPTY motif form an antiparallel beta-sheet with the beta5 strand of the PID domain, the binding mode typically observed in the PID/PTB.peptide complex. On the other hand, the N-terminal region of the peptide forms a 2.5-turn alpha-helix and interacts extensively with the C-terminal alpha-helix and the peripheral regions of the PID domain, representing a novel mode of peptide binding that has not been reported previously for the PID/PTB.peptide complex. The indispensability of the N-terminal region of the peptide for the high affinity of the PID-peptide interaction is consistent with NMR titration and isothermal calorimetry data. The extensive binding features of the PID domain of Fe65L1 with the cytoplasmic domain of APP provide a framework for further understanding of the function, trafficking, and processing of APP modulated by adapter proteins.
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===Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L===
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Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode.,Li H, Koshiba S, Hayashi F, Tochio N, Tomizawa T, Kasai T, Yabuki T, Motoda Y, Harada T, Watanabe S, Inoue M, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S J Biol Chem. 2008 Oct 3;283(40):27165-78. Epub 2008 Jul 23. PMID:18650440<ref>PMID:18650440</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18650440}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2yt0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18650440 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18650440}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2YT0 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YT0 OCA].
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==Reference==
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<ref group="xtra">PMID:18650440</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Harada, T.]]
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[[Category: Harada T]]
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[[Category: Kigawa, T.]]
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[[Category: Kigawa T]]
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[[Category: Koshiba, S.]]
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[[Category: Koshiba S]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Tochio N]]
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[[Category: Tochio, N.]]
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[[Category: Watanabe S]]
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[[Category: Watanabe, S.]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S.]]
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[[Category: Amyloid precursor protein]]
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[[Category: Chimera]]
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[[Category: Fe65l]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Pid domain]]
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[[Category: Protein binding]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:30:46 2009''
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Current revision

Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L

PDB ID 2yt0

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