2gph
From Proteopedia
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{{STRUCTURE_2gph| PDB=2gph | SCENE= }} | {{STRUCTURE_2gph| PDB=2gph | SCENE= }} | ||
===Docking motif interactions in the MAP kinase ERK2=== | ===Docking motif interactions in the MAP kinase ERK2=== | ||
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{{ABSTRACT_PUBMED_16765894}} | {{ABSTRACT_PUBMED_16765894}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2gph]] is a 2 chain structure of [[Mitogen-activated protein kinase]] and [[Tyrosine phosphatase]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPH OCA]. | |
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| + | ==See Also== | ||
| + | *[[Mitogen-activated protein kinase|Mitogen-activated protein kinase]] | ||
| + | *[[Tyrosine phosphatase|Tyrosine phosphatase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016765894</ref><ref group="xtra">PMID:019053285</ref><references group="xtra"/> |
[[Category: Mitogen-activated protein kinase]] | [[Category: Mitogen-activated protein kinase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: Phosphatase-derived peptide]] | [[Category: Phosphatase-derived peptide]] | ||
[[Category: Processing conformation]] | [[Category: Processing conformation]] | ||
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Revision as of 16:47, 25 July 2012
Contents |
Docking motif interactions in the MAP kinase ERK2
Template:ABSTRACT PUBMED 16765894
About this Structure
2gph is a 2 chain structure of Mitogen-activated protein kinase and Tyrosine phosphatase with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Zhou T, Sun L, Humphreys J, Goldsmith EJ. Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure. 2006 Jun;14(6):1011-9. PMID:16765894 doi:10.1016/j.str.2006.04.006
- Critton DA, Tortajada A, Stetson G, Peti W, Page R. Structural basis of substrate recognition by hematopoietic tyrosine phosphatase. Biochemistry. 2008 Dec 16;47(50):13336-45. PMID:19053285 doi:10.1021/bi801724n
