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2itt
From Proteopedia
| Line 20: | Line 20: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2ITT is a | + | 2ITT is a 1 chain structure of 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=2ITT OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:17349580</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
| - | [[Category: Single protein]] | ||
[[Category: Boggon, T J.]] | [[Category: Boggon, T J.]] | ||
[[Category: Eck, M J.]] | [[Category: Eck, M J.]] | ||
| Line 54: | Line 53: | ||
[[Category: Tyrosine-protein kinase]] | [[Category: Tyrosine-protein kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:29:51 2009'' |
Revision as of 09:29, 17 February 2009
CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX WITH AEE788
Template:ABSTRACT PUBMED 17349580
About this Structure
2ITT is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Yun CH, Boggon TJ, Li Y, Woo MS, Greulich H, Meyerson M, Eck MJ. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell. 2007 Mar;11(3):217-27. PMID:17349580 doi:http://dx.doi.org/10.1016/j.ccr.2006.12.017
Page seeded by OCA on Tue Feb 17 11:29:51 2009
Categories: Homo sapiens | Receptor protein-tyrosine kinase | Boggon, T J. | Eck, M J. | Greulich, H. | Li, Y. | Meyerson, M. | Woo, S. | Yun, C H. | Aee788 | Alternative splicing | Anti-oncogene | Atp-binding | Cell cycle | Disease mutation | Egfr | Epidermal growth factor | Glycoprotein | Kinase | L858r | Membrane | Nucleotide-binding | Phosphorylation | Polymorphism | Receptor | Transferase | Transmembrane | Tyrosine-protein kinase
