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2r0b

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Revision as of 07:39, 25 October 2017

Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein

Structural highlights

2r0b is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	STYX (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[STYX_HUMAN] Catalytically inactive phosphatase. Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2). Seems to play a role in spermiogenesis (By similarity).

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.

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r0b"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein==
 <StructureSection load='2r0b' size='340' side='right' caption='[[2r0b]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STYX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2r0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0b OCA], [http://pdbe.org/2r0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r0b RCSB], [http://www.ebi.ac.uk/pdbsum/2r0b PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2r0b TOPSAN]</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=2r0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0b OCA], [http://pdbe.org/2r0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r0b RCSB], [http://www.ebi.ac.uk/pdbsum/2r0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0b ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2r0b TOPSAN]</span></td></tr>
 </table>
 == Function ==

2r0b

From Proteopedia

Revision as of 07:39, 25 October 2017

Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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