2vew: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR== | ==CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR== | ||
<StructureSection load='2vew' size='340' side='right' caption='[[2vew]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2vew' size='340' side='right'caption='[[2vew]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vew]] is a 1 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=2VEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VEW FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vew]] is a 1 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=2VEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VEW FirstGlance]. <br> | ||
Line 15: | Line 15: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/2vew_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/2vew_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Line 30: | Line 30: | ||
</div> | </div> | ||
<div class="pdbe-citations 2vew" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2vew" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosine phosphatase|Tyrosine phosphatase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Line 35: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Ala, P J]] | [[Category: Ala, P J]] |
Revision as of 10:16, 21 August 2019
CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITORCRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR
Structural highlights
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 PubMedThe structure-based design and synthesis of isothiazolidinone (IZD) inhibitors of PTP1B containing imidazoles and imidazolines and their modification to interact with the B site of PTP1B are described here. The X-ray crystal structures of 3I and 4I complexed with PTP1B were solved and revealed the inhibitors are interacting extensively with the B site of the enzyme. Isothiazolidinone inhibitors of PTP1B containing imidazoles and imidazolines.,Douty B, Wayland B, Ala PJ, Bower MJ, Pruitt J, Bostrom L, Wei M, Klabe R, Gonneville L, Wynn R, Burn TC, Liu PC, Combs AP, Yue EW Bioorg Med Chem Lett. 2008 Jan 1;18(1):66-71. Epub 2007 Nov 9. PMID:18037290[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|