1i8g: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /> <applet load="1i8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8g" /> '''SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLE...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1i8g.gif|left|200px]]<br />
<applet load="1i8g" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1i8g" />
'''SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE'''<br />


==Overview==
==SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE==
The recent crystal structure of Pin1 protein bound to a doubly, phosphorylated peptide from the C-terminal domain of RNA polymerase II, revealed that binding interactions between Pin1 and its substrate take, place through its Trp-Trp (WW) domain at the level of the loop, Ser(11)-Arg(12) and the aromatic pair Tyr(18)-Trp(29), and showed a trans, conformation for both pSer-Pro peptide bonds. However, the orientation of, the ligand in the aromatic recognition groove still could be, sequence-specific, as previously observed in SH3 domains complexed by, peptide ligands or for different class of WW domains (Zarrinpar, A., and, Lim, W. A. (2000) Nat. Struct. Biol. 7, 611-613). Because the bound, peptide conformation could also differ as observed for peptide ligands, bound to the 14-3-3 domain, ligand orientation and conformation for two, other biologically relevant monophosphate substrates, one derived from the, Cdc25 phosphatase of Xenopus laevis (EQPLpTPVTDL) and another from the, human tau protein (KVSVVRpTPPKSPS) in complex with the WW domain are here, studied by solution NMR methods. First, the proton resonance perturbations, on the WW domain upon complexation with both peptide ligands were, determined to be essentially located in the positively charged, beta-hairpin Ser(11)-Gly(15) and around the aromatic Trp(29). Dissociation, equilibrium constants of 117 and 230 microm for Cdc25 and tau peptides, respectively, were found. Several intermolecular nuclear Overhauser, effects between WW domain and substrates were obtained from a, ligand-saturated solution and were used to determine the structures of the, complexes in solution. We found a similar N to C orientation as the one, observed in the crystal complex structure of Pin1 and a trans conformation, for the pThr-Pro peptidic bond in both peptide ligands, thereby indicating, a unique binding scheme for the Pin1 WW domain to its multiple substrates.
<StructureSection load='1i8g' size='340' side='right'caption='[[1i8g]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i8g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I8G FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=1i8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i8g OCA], [https://pdbe.org/1i8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i8g RCSB], [https://www.ebi.ac.uk/pdbsum/1i8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i8g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MPIP3_XENLA MPIP3_XENLA] This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.
== 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/i8/1i8g_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=1i8g ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1I8G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I8G OCA].
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides., Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buee L, Lippens G, Landrieu I, J Biol Chem. 2001 Jul 6;276(27):25150-6. Epub 2001 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11313338 11313338]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Xenopus laevis]]
[[Category: Drobecq, H.]]
[[Category: Drobecq H]]
[[Category: Landrieu, I.]]
[[Category: Landrieu I]]
[[Category: Lippens, G.]]
[[Category: Lippens G]]
[[Category: Wieruszeski, J.M.]]
[[Category: Wieruszeski J-M]]
[[Category: Wintjens, R.]]
[[Category: Wintjens R]]
[[Category: cell division]]
[[Category: nuclear protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:27:26 2007''

Latest revision as of 07:45, 3 April 2024

SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1i8g&oldid=4120534"