2itn: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2ITN is a | 2ITN 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=2ITN 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: Boggon, T J.]] | [[Category: Boggon, T J.]] | ||
[[Category: Eck, M J.]] | [[Category: Eck, M J.]] | ||
| Line 55: | Line 54: | ||
[[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 00:29:14 2009'' | ||
Revision as of 22:29, 16 February 2009
CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH AMP-PNP
Template:ABSTRACT PUBMED 17349580
About this Structure
2ITN 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:https://dx.doi.org/10.1016/j.ccr.2006.12.017
Page seeded by OCA on Tue Feb 17 00:29:14 2009
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- Homo sapiens
- Receptor protein-tyrosine kinase
- Boggon, T J.
- Eck, M J.
- Greulich, H.
- Li, Y.
- Meyerson, M.
- Woo, S.
- Yun, C H.
- Alternative splicing
- Amp-pnp
- Anp
- Anti-oncogene
- Atp-binding
- Cell cycle
- Disease mutation
- Egfr
- Epidermal growth factor
- G719
- Glycoprotein
- Kinase
- Membrane
- Nucleotide-binding
- Phosphorylation
- Polymorphism
- Receptor
- Transferase
- Transmembrane
- Tyrosine-protein kinase
