2nnt: Difference between revisions

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[[Image:2nnt.png|left|200px]]


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==General structural motifs of amyloid protofilaments==
The line below this paragraph, containing "STRUCTURE_2nnt", creates the "Structure Box" on the page.
<StructureSection load='2nnt' size='340' side='right'caption='[[2nnt]]' 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'>[[2nnt]] is a 4 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=2NNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNT 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">Solid-state 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=2nnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnt OCA], [https://pdbe.org/2nnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnt RCSB], [https://www.ebi.ac.uk/pdbsum/2nnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnt ProSAT]</span></td></tr>
{{STRUCTURE_2nnt|  PDB=2nnt  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/TCRG1_HUMAN TCRG1_HUMAN] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.<ref>PMID:9315662</ref> <ref>PMID:11604498</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/2nnt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2nnt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human CA150, a transcriptional activator, binds to and is co-deposited with huntingtin during Huntington's disease. The second WW domain of CA150 is a three-stranded beta-sheet that folds in vitro in microseconds and forms amyloid fibers under physiological conditions. We found from exhaustive alanine scanning studies that fibrillation of this WW domain begins from its denatured conformations, and we identified a subset of residues critical for fibril formation. We used high-resolution magic-angle-spinning NMR studies on site-specific isotopically labeled fibrils to identify abundant long-range interactions between side chains. The distribution of critical residues identified by the alanine scanning and NMR spectroscopy, along with the electron microscopy data, revealed the protofilament repeat unit: a 26-residue non-native beta-hairpin. The structure we report has similarities to the hairpin formed by the A(beta)((1-40)) protofilament, yet also contains closely packed side-chains in a "steric zipper" arrangement found in the cross-beta spine formed from small peptides from the Sup35 prion protein. Fibrillation of unrelated amyloidogenic sequences shows the common feature of zippered repeat units that act as templates for fiber elongation.


===General structural motifs of amyloid protofilaments===
General structural motifs of amyloid protofilaments.,Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16248-53. Epub 2006 Oct 23. PMID:17060612<ref>PMID:17060612</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_17060612}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2nnt" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 17060612 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17060612}}
__TOC__
 
</StructureSection>
==About this Structure==
2NNT is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNT OCA].
 
==Reference==
<ref group="xtra">PMID:17060612</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Becker, J.]]
[[Category: Large Structures]]
[[Category: Berriman, J.]]
[[Category: Becker J]]
[[Category: Ferguson, N.]]
[[Category: Berriman J]]
[[Category: Fersht, A R.]]
[[Category: Ferguson N]]
[[Category: Flinders, J.]]
[[Category: Fersht AR]]
[[Category: Krause, G.]]
[[Category: Flinders J]]
[[Category: Oschkinat, H.]]
[[Category: Krause G]]
[[Category: Petrovich, M.]]
[[Category: Oschkinat H]]
[[Category: Sharpe, T D.]]
[[Category: Petrovich M]]
[[Category: Tidow, H.]]
[[Category: Sharpe TD]]
[[Category: Tremmel, S.]]
[[Category: Tidow H]]
[[Category: Beta-hairpin]]
[[Category: Tremmel S]]
[[Category: Ca150 second ww domain]]
[[Category: Fbp28 protofilament]]
[[Category: Fibre]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:47:58 2009''

Latest revision as of 03:09, 28 December 2023

General structural motifs of amyloid protofilamentsGeneral structural motifs of amyloid protofilaments

Structural highlights

2nnt is a 4 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:Solid-state NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TCRG1_HUMAN Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human CA150, a transcriptional activator, binds to and is co-deposited with huntingtin during Huntington's disease. The second WW domain of CA150 is a three-stranded beta-sheet that folds in vitro in microseconds and forms amyloid fibers under physiological conditions. We found from exhaustive alanine scanning studies that fibrillation of this WW domain begins from its denatured conformations, and we identified a subset of residues critical for fibril formation. We used high-resolution magic-angle-spinning NMR studies on site-specific isotopically labeled fibrils to identify abundant long-range interactions between side chains. The distribution of critical residues identified by the alanine scanning and NMR spectroscopy, along with the electron microscopy data, revealed the protofilament repeat unit: a 26-residue non-native beta-hairpin. The structure we report has similarities to the hairpin formed by the A(beta)((1-40)) protofilament, yet also contains closely packed side-chains in a "steric zipper" arrangement found in the cross-beta spine formed from small peptides from the Sup35 prion protein. Fibrillation of unrelated amyloidogenic sequences shows the common feature of zippered repeat units that act as templates for fiber elongation.

General structural motifs of amyloid protofilaments.,Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16248-53. Epub 2006 Oct 23. PMID:17060612[3]

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

References

  1. Sune C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA. CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. Mol Cell Biol. 1997 Oct;17(10):6029-39. PMID:9315662
  2. Goldstrohm AC, Albrecht TR, Sune C, Bedford MT, Garcia-Blanco MA. The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Mol Cell Biol. 2001 Nov;21(22):7617-28. PMID:11604498 doi:10.1128/MCB.21.22.7617-7628.2001
  3. Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR. General structural motifs of amyloid protofilaments. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16248-53. Epub 2006 Oct 23. PMID:17060612
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