1rxd: Difference between revisions

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==Crystal structure of human protein tyrosine phosphatase 4A1==
==Crystal structure of human protein tyrosine phosphatase 4A1==
<StructureSection load='1rxd' size='340' side='right' caption='[[1rxd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1rxd' size='340' side='right'caption='[[1rxd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1rxd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RXD FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXD FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxd OCA], [http://pdbe.org/1rxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rxd RCSB], [http://www.ebi.ac.uk/pdbsum/1rxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxd ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1rxd TOPSAN]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1rxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxd OCA], [https://pdbe.org/1rxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxd RCSB], [https://www.ebi.ac.uk/pdbsum/1rxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxd ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1rxd TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TP4A1_HUMAN TP4A1_HUMAN]] Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis.<ref>PMID:12235145</ref> <ref>PMID:14643450</ref> <ref>PMID:12782572</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxd_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rxd_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Tyrosine phosphatase|Tyrosine phosphatase]]
*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Almo SC]]
[[Category: Burley, S K]]
[[Category: Burley SK]]
[[Category: Fedorov, A A]]
[[Category: Fedorov AA]]
[[Category: Structural genomic]]
[[Category: Sun JP]]
[[Category: Sun, J P]]
[[Category: Zhang ZY]]
[[Category: Zhang, Z Y]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Unknown function]]

Latest revision as of 03:27, 21 November 2024

Crystal structure of human protein tyrosine phosphatase 4A1Crystal structure of human protein tyrosine phosphatase 4A1

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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

The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.

Structural genomics of protein phosphatases.,Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037[1]

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

See Also

References

  1. Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK. Structural genomics of protein phosphatases. J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037 doi:http://dx.doi.org/10.1007/s10969-007-9036-1

1rxd, resolution 1.90Å

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