2edx: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 1: Line 1:


==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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[2edx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</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='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'>[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>
<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 ==
[[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>
[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]]
Line 27: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Inoue M]]
[[Category: Inoue, M]]
[[Category: Kigawa T]]
[[Category: Kigawa, T]]
[[Category: Koshiba S]]
[[Category: Koshiba, S]]
[[Category: Sato M]]
[[Category: Structural genomic]]
[[Category: Yokoyama S]]
[[Category: Sato, M]]
[[Category: Yokoyama, S]]
[[Category: Ec 3 1.3 48]]
[[Category: Lar protein]]
[[Category: Leukocyte antigen related]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rsgi]]
[[Category: Signaling protein]]

Latest revision as of 21:50, 29 May 2024

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 Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
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
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA