1erk
From Proteopedia
(New page: 200px<br /><applet load="1erk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1erk, resolution 2.3Å" /> '''STRUCTURE OF SIGNAL-R...) |
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| - | [[Image:1erk.gif|left|200px]]<br /><applet load="1erk" size=" | + | [[Image:1erk.gif|left|200px]]<br /><applet load="1erk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1erk, resolution 2.3Å" /> | caption="1erk, resolution 2.3Å" /> | ||
'''STRUCTURE OF SIGNAL-REGULATED KINASE'''<br /> | '''STRUCTURE OF SIGNAL-REGULATED KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the MAP kinase ERK2, a ubiquitous protein kinase target | + | The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes. |
==About this Structure== | ==About this Structure== | ||
| - | 1ERK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1ERK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1ERK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Goldsmith, E | + | [[Category: Goldsmith, E J.]] |
| - | [[Category: Harkins, P | + | [[Category: Harkins, P C.]] |
[[Category: atp-binding cell cycle]] | [[Category: atp-binding cell cycle]] | ||
[[Category: phosphorylation.]] | [[Category: phosphorylation.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:43 2008'' |
Revision as of 10:30, 21 February 2008
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STRUCTURE OF SIGNAL-REGULATED KINASE
Overview
The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.
About this Structure
1ERK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution., Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ, Nature. 1994 Feb 24;367(6465):704-11. PMID:8107865
Page seeded by OCA on Thu Feb 21 12:30:43 2008
