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1wax

From Proteopedia

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Protein tyrosine phosphatase 1B with active site inhibitor

Structural highlights

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

Function

PTN1_HUMAN Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.^[1] ^[2]

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

Fragment screening offers an alternative to traditional screening for discovering new leads in drug discovery programs. This paper describes a fragment screening methodology based on high throughput X-ray crystallography. The method is illustrated against five proteins (p38 MAP kinase, CDK2, thrombin, ribonuclease A, and PTP1B). The fragments identified have weak potency (>100 microM) but are efficient binders relative to their size and may therefore represent suitable starting points for evolution to good quality lead compounds. The examples illustrate that a range of molecular interactions (i.e., lipophilic, charge-charge, neutral hydrogen bonds) can drive fragment binding and also that fragments can induce protein movement. We believe that the method has great potential for the discovery of novel lead compounds against a range of targets, and the companion paper illustrates how lead compounds have been identified for p38 MAP kinase starting from fragments such as those described in this paper.

Fragment-based lead discovery using X-ray crystallography.,Hartshorn MJ, Murray CW, Cleasby A, Frederickson M, Tickle IJ, Jhoti H J Med Chem. 2005 Jan 27;48(2):403-13. PMID:15658854^[3]

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

References

↑ Nievergall E, Janes PW, Stegmayer C, Vail ME, Haj FG, Teng SW, Neel BG, Bastiaens PI, Lackmann M. PTP1B regulates Eph receptor function and trafficking. J Cell Biol. 2010 Dec 13;191(6):1189-203. doi: 10.1083/jcb.201005035. Epub 2010, Dec 6. PMID:21135139 doi:10.1083/jcb.201005035
↑ Krishnan N, Fu C, Pappin DJ, Tonks NK. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal. 2011 Dec 13;4(203):ra86. doi: 10.1126/scisignal.2002329. PMID:22169477 doi:10.1126/scisignal.2002329
↑ Hartshorn MJ, Murray CW, Cleasby A, Frederickson M, Tickle IJ, Jhoti H. Fragment-based lead discovery using X-ray crystallography. J Med Chem. 2005 Jan 27;48(2):403-13. PMID:15658854 doi:http://dx.doi.org/10.1021/jm0495778

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wax"

@@ Line 3: / Line 3: @@
 <StructureSection load='1wax' size='340' side='right'caption='[[1wax]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wax]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WAX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wax]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LO1:[[4-(AMINOMETHYL)PHENYL]AMINO]OXO-ACETIC+ACID,'>LO1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a5y|1a5y]], [[1aax|1aax]], [[1bzc|1bzc]], [[1bzh|1bzh]], [[1bzj|1bzj]], [[1c83|1c83]], [[1c84|1c84]], [[1c85|1c85]], [[1c86|1c86]], [[1c87|1c87]], [[1c88|1c88]], [[1ecv|1ecv]], [[1een|1een]], [[1eeo|1eeo]], [[1g1f|1g1f]], [[1g1g|1g1g]], [[1g1h|1g1h]], [[1g7f|1g7f]], [[1g7g|1g7g]], [[1gfy|1gfy]], [[1i57|1i57]], [[1jf7|1jf7]], [[1kak|1kak]], [[1kav|1kav]], [[1l8g|1l8g]], [[1lqf|1lqf]], [[1nl9|1nl9]], [[1nny|1nny]], [[1no6|1no6]], [[1nwe|1nwe]], [[1nwl|1nwl]], [[1nz7|1nz7]], [[1oem|1oem]], [[1oeo|1oeo]], [[1oes|1oes]], [[1oet|1oet]], [[1oeu|1oeu]], [[1oev|1oev]], [[1ony|1ony]], [[1onz|1onz]], [[1pa1|1pa1]], [[1ph0|1ph0]], [[1ptt|1ptt]], [[1ptu|1ptu]], [[1ptv|1ptv]], [[1pty|1pty]], [[1pxh|1pxh]], [[1pyn|1pyn]], [[1q1m|1q1m]], [[1q6j|1q6j]], [[1q6m|1q6m]], [[1q6n|1q6n]], [[1q6p|1q6p]], [[1q6s|1q6s]], [[1q6t|1q6t]], [[1qxk|1qxk]], [[1sug|1sug]], [[1t48|1t48]], [[1t49|1t49]], [[1t4j|1t4j]], [[1xbo|1xbo]], [[2hnp|2hnp]], [[2hnq|2hnq]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LO1:[[4-(AMINOMETHYL)PHENYL]AMINO]OXO-ACETIC+ACID,'>LO1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wax OCA], [https://pdbe.org/1wax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wax RCSB], [https://www.ebi.ac.uk/pdbsum/1wax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wax ProSAT]</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=1wax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wax OCA], [http://pdbe.org/1wax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wax RCSB], [http://www.ebi.ac.uk/pdbsum/1wax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wax ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN]] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
+[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Cleasby A]]
-[[Category: Cleasby, A]]
+[[Category: Frederickson M]]
-[[Category: Frederickson, M]]
+[[Category: Hartshorn MJ]]
-[[Category: Hartshorn, M J]]
+[[Category: Jhoti H]]
-[[Category: Jhoti, H]]
+[[Category: Murray CW]]
-[[Category: Murray, C W]]
+[[Category: Tickle IJ]]
-[[Category: Tickle, I J]]
-[[Category: Acetylation]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Phosphorylation]]
-[[Category: Protein tyrosine phosphatase]]

1wax

From Proteopedia

Current revision

Protein tyrosine phosphatase 1B with active site inhibitor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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