2edx: Difference between revisions

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==Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F==
==Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F==
<StructureSection load='2edx' size='340' side='right' caption='[[2edx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2edx' size='340' side='right'caption='[[2edx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2edx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EDX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2edx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EDX FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=2edx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2edx OCA], [http://pdbe.org/2edx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2edx RCSB], [http://www.ebi.ac.uk/pdbsum/2edx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2edx ProSAT], [http://www.topsan.org/Proteins/RSGI/2edx TOPSAN]</span></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=2edx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2edx OCA], [https://pdbe.org/2edx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2edx RCSB], [https://www.ebi.ac.uk/pdbsum/2edx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2edx ProSAT], [https://www.topsan.org/Proteins/RSGI/2edx TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PTPRF_HUMAN PTPRF_HUMAN]] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).<ref>PMID:10338209</ref>  The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.<ref>PMID:10338209</ref>   
[[https://www.uniprot.org/uniprot/PTPRF_HUMAN PTPRF_HUMAN]] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).<ref>PMID:10338209</ref>  The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.<ref>PMID:10338209</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Tyrosine phosphatase|Tyrosine phosphatase]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Inoue, M]]
[[Category: Inoue, M]]

Revision as of 15:01, 10 February 2021

Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase FSolution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F

Structural highlights

2edx is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:PTPRF (HUMAN)
Activity:Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[PTPRF_HUMAN] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).[1] The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.[2]

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. Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
  2. Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
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