1a17: Difference between revisions

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[[Image:1a17.gif|left|200px]]


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==TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5==
The line below this paragraph, containing "STRUCTURE_1a17", creates the "Structure Box" on the page.
<StructureSection load='1a17' size='340' side='right'caption='[[1a17]], [[Resolution|resolution]] 2.45&Aring;' 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'>[[1a17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A17 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">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1a17| PDB=1a17 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a17 OCA], [https://pdbe.org/1a17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a17 RCSB], [https://www.ebi.ac.uk/pdbsum/1a17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a17 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPP5_HUMAN PPP5_HUMAN] May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1.
== 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/a1/1a17_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=1a17 ConSurf].
<div style="clear:both"></div>


'''TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5'''
==See Also==
 
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a wide variety of proteins, present in tandem arrays of 3-16 motifs, which form scaffolds to mediate protein-protein interactions and often the assembly of multiprotein complexes. TPR-containing proteins include the anaphase promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67 phox, hsp90-binding immunophilins, transcription factors, the PKR protein kinase inhibitor, and peroxisomal and mitochondrial import proteins. Here, we report the crystal structure of the TPR domain of a protein phosphatase, PP5. Each of the three TPR motifs of this domain consist of a pair of antiparallel alpha-helices of equivalent length. Adjacent TPR motifs are packed together in a parallel arrangement such that a tandem TPR motif structure is composed of a regular series of antiparallel alpha-helices. The uniform angular and spatial arrangement of neighbouring alpha-helices defines a helical structure and creates an amphipathic groove. Multiple-TPR motif proteins would fold into a right-handed super-helical structure with a continuous helical groove suitable for the recognition of target proteins, hence defining a novel mechanism for protein recognition. The spatial arrangement of alpha-helices in the PP5-TPR domain is similar to those within 14-3-3 proteins.
 
==About this Structure==
1A17 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=1A17 OCA].
 
==Reference==
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions., Das AK, Cohen PW, Barford D, EMBO J. 1998 Mar 2;17(5):1192-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9482716 9482716]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Barford D]]
[[Category: Barford, D.]]
[[Category: Cohen PTW]]
[[Category: Cohen, P T.W.]]
[[Category: Das AK]]
[[Category: Das, A K.]]
[[Category: Hydrolase]]
[[Category: Phosphatase]]
[[Category: Protein-protein interaction]]
[[Category: Super-helix]]
[[Category: Tpr]]
[[Category: X-ray structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:39:27 2008''

Latest revision as of 06:26, 7 February 2024

TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5

1a17, resolution 2.45Å

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