1ayd: Difference between revisions

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New page: left|200px<br /><applet load="1ayd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayd, resolution 2.2Å" /> '''CRYSTAL STRUCTURES OF...
 
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[[Image:1ayd.jpg|left|200px]]<br /><applet load="1ayd" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE'''<br />


==Overview==
==CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE==
BACKGROUND: Src homology 2 (SH2) domains bind to phosphotyrosine residues, in a sequence-specific manner, and thereby couple tyrosine phosphorylation, to changes in the localization or catalytic activity of signal transducing, molecules. Current understanding of SH2 specificity is based on the, structures of SH2-peptide complexes of the closely-related Src and Lck, tyrosine kinases. The tyrosine phosphatase Syp contains two SH2 domains, that are relatively divergent from those of the tyrosine kinases, with, distinct target specificities, and is thus well suited for structural, studies aimed at extending our understanding of SH2 specificity. RESULTS:, Crystal structures of the amino-terminal SH2 domain of Syp in separate, complexes with two high-affinity peptides, in complex with a non-specific, peptide and in the uncomplexed form have been determined at between 2 A, and 3 A resolution. The structure of the SH2 domain and the mode of, high-affinity peptide binding is essentially similar to that seen in the, Src and Lck structures. However, the binding interface is more extensive, in Syp. CONCLUSIONS: Most SH2 targets have hydrophobic residues at the, third position following the phosphotyrosine, and the Syp structure, confirms that the peptide is anchored to the SH2 surface by this residue, and by the phosphotyrosine. In addition, the Syp structure has revealed, that sequence specificity can extend across the five residues following, the phosphotyrosine, and has shown how the SH2 domain's surface topography, can be altered with resulting changes in specificity, while conserving the, structure of the central core of the domain.
<StructureSection load='1ayd' size='340' side='right'caption='[[1ayd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ayd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1ayd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayd OCA], [https://pdbe.org/1ayd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayd RCSB], [https://www.ebi.ac.uk/pdbsum/1ayd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTN11_MOUSE PTN11_MOUSE] Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity (By similarity).<ref>PMID:14967142</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/ay/1ayd_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=1ayd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AYD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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=1AYD OCA].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase., Lee CH, Kominos D, Jacques S, Margolis B, Schlessinger J, Shoelson SE, Kuriyan J, Structure. 1994 May 15;2(5):423-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7521735 7521735]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Kuriyan J]]
[[Category: Single protein]]
[[Category: Lee C-H]]
[[Category: Kuriyan, J.]]
[[Category: Lee, C.H.]]
[[Category: hydrolase(sh2 domain)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:12:20 2007''

Latest revision as of 09:34, 7 February 2024

CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASECRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE

Structural highlights

1ayd is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTN11_MOUSE Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity (By similarity).[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Zhang SQ, Yang W, Kontaridis MI, Bivona TG, Wen G, Araki T, Luo J, Thompson JA, Schraven BL, Philips MR, Neel BG. Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment. Mol Cell. 2004 Feb 13;13(3):341-55. PMID:14967142

1ayd, resolution 2.20Å

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