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[[ | ==Drug resistant cSrc kinase domain in complex with covalent inhibitor PD168393== | ||
<StructureSection load='3lok' size='340' side='right' caption='[[3lok]], [[Resolution|resolution]] 2.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lok]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LOK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DJK:N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE'>DJK</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hwp|2hwp]], [[2qlq|2qlq]], [[2qq7|2qq7]], [[2qi8|2qi8]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRC, v-Src sarcoma viral oncogene ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </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=3lok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lok OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lok RCSB], [http://www.ebi.ac.uk/pdbsum/3lok PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Targeting protein kinases in cancer therapy with irreversible small-molecule inhibitors is moving to the forefront of kinase-inhibitor research and is thought to be an effective means of overcoming mutation-associated drug resistance in epidermal growth factor receptor kinase (EGFR). We generated a detection technique that allows direct measurements of covalent bond formation without relying on kinase activity, thereby allowing the straightforward investigation of the influence of steric clashes on covalent inhibitors in different resistant kinase mutants. The obtained results are discussed together with structural biology and biochemical studies of catalytic activity in both wild-type and gatekeeper mutated kinase variants to draw conclusions about the impact of steric hindrance and increased catalytic activity in drug-resistant kinase variants. | |||
Characterization of irreversible kinase inhibitors by directly detecting covalent bond formation: a tool for dissecting kinase drug resistance.,Kluter S, Simard JR, Rode HB, Grutter C, Pawar V, Raaijmakers HC, Barf TA, Rabiller M, van Otterlo WA, Rauh D Chembiochem. 2010 Dec 10;11(18):2557-66. PMID:21080395<ref>PMID:21080395</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Tyrosine kinase|Tyrosine kinase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Non-specific protein-tyrosine kinase]] | [[Category: Non-specific protein-tyrosine kinase]] | ||
[[Category: Gruetter, C | [[Category: Gruetter, C]] | ||
[[Category: Rauh, D | [[Category: Rauh, D]] | ||
[[Category: Rode, H B | [[Category: Rode, H B]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Covalent inhibitor]] | [[Category: Covalent inhibitor]] | ||
Revision as of 12:04, 9 December 2014
Drug resistant cSrc kinase domain in complex with covalent inhibitor PD168393Drug resistant cSrc kinase domain in complex with covalent inhibitor PD168393
Structural highlights
Publication Abstract from PubMedTargeting protein kinases in cancer therapy with irreversible small-molecule inhibitors is moving to the forefront of kinase-inhibitor research and is thought to be an effective means of overcoming mutation-associated drug resistance in epidermal growth factor receptor kinase (EGFR). We generated a detection technique that allows direct measurements of covalent bond formation without relying on kinase activity, thereby allowing the straightforward investigation of the influence of steric clashes on covalent inhibitors in different resistant kinase mutants. The obtained results are discussed together with structural biology and biochemical studies of catalytic activity in both wild-type and gatekeeper mutated kinase variants to draw conclusions about the impact of steric hindrance and increased catalytic activity in drug-resistant kinase variants. Characterization of irreversible kinase inhibitors by directly detecting covalent bond formation: a tool for dissecting kinase drug resistance.,Kluter S, Simard JR, Rode HB, Grutter C, Pawar V, Raaijmakers HC, Barf TA, Rabiller M, van Otterlo WA, Rauh D Chembiochem. 2010 Dec 10;11(18):2557-66. PMID:21080395[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Gallus gallus
- Non-specific protein-tyrosine kinase
- Gruetter, C
- Rauh, D
- Rode, H B
- Atp-binding
- Covalent inhibitor
- Drug resistance
- Irreversible inhibitor
- Kinase
- Lipoprotein
- Myristate
- Nucleotide-binding
- Pd168393
- Phosphoprotein
- Proto-oncogene
- Sh2 domain
- Sh3 domain
- Src kinase domain
- Transferase-transferase inhibitor complex
- Tyrosine-protein kinase