2vwu: Difference between revisions

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[[Image:2vwu.png|left|200px]]
==EPHB4 KINASE DOMAIN INHIBITOR COMPLEX==
<StructureSection load='2vwu' size='340' side='right' caption='[[2vwu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vwu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWU FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7X1:N-(5-CHLORO-1,3-BENZODIOXOL-4-YL)-6-METHOXY-7-(3-PIPERIDIN-1-YLPROPOXY)QUINAZOLIN-4-AMINE'>7X1</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bba|2bba]], [[2vwv|2vwv]], [[2vwy|2vwy]], [[2vww|2vww]], [[2vwx|2vwx]], [[2vwz|2vwz]], [[2vx0|2vx0]], [[2vx1|2vx1]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vwu RCSB], [http://www.ebi.ac.uk/pdbsum/2vwu PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vw/2vwu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A series of bis-anilinopyrimidines have been identified as potent inhibitors of the tyrosine kinase EphB4. Structural information from two alternative series identified from screening efforts was combined to identify the initial leads.


{{STRUCTURE_2vwu|  PDB=2vwu  |  SCENE=  }}
Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines.,Bardelle C, Cross D, Davenport S, Kettle JG, Ko EJ, Leach AG, Mortlock A, Read J, Roberts NJ, Robins P, Williams EJ Bioorg Med Chem Lett. 2008 May 1;18(9):2776-80. Epub 2008 Apr 10. PMID:18434142<ref>PMID:18434142</ref>


===EPHB4 KINASE DOMAIN INHIBITOR COMPLEX===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_18434142}}
 
==About this Structure==
[[2vwu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VWU OCA].


==See Also==
==See Also==
*[[Ephrin receptor|Ephrin receptor]]
*[[Ephrin receptor|Ephrin receptor]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018434142</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Receptor protein-tyrosine kinase]]
[[Category: Receptor protein-tyrosine kinase]]

Revision as of 08:46, 29 September 2014

EPHB4 KINASE DOMAIN INHIBITOR COMPLEX

2vwu, resolution 2.00Å

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