2erk
From Proteopedia
(New page: 200px<br /><applet load="2erk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2erk, resolution 2.4Å" /> '''PHOSPHORYLATED MAP KI...) |
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| - | [[Image:2erk.jpg|left|200px]]<br /><applet load="2erk" size=" | + | [[Image:2erk.jpg|left|200px]]<br /><applet load="2erk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2erk, resolution 2.4Å" /> | caption="2erk, resolution 2.4Å" /> | ||
'''PHOSPHORYLATED MAP KINASE ERK2'''<br /> | '''PHOSPHORYLATED MAP KINASE ERK2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the | + | The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase insertion, the C-terminal extension, and helix C. Domain rotation and remodeling of the proline-directed P+1 specificity pocket account for the activation. The conformation of the P+1 pocket is similar to a second proline-directed kinase, CDK2-CyclinA, thus permitting the origin of this specificity to be defined. Conformational changes outside the lip provide loci at which the state of phosphorylation can be felt by other cellular components. |
==About this Structure== | ==About this Structure== | ||
| - | 2ERK 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:// | + | 2ERK 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=2ERK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Canagarajah, B | + | [[Category: Canagarajah, B J.]] |
| - | [[Category: Goldsmith, E | + | [[Category: Goldsmith, E J.]] |
[[Category: kinase]] | [[Category: kinase]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
[[Category: serine/threonine-protein kinase]] | [[Category: serine/threonine-protein kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:51 2008'' |
Revision as of 15:13, 21 February 2008
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PHOSPHORYLATED MAP KINASE ERK2
Overview
The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase insertion, the C-terminal extension, and helix C. Domain rotation and remodeling of the proline-directed P+1 specificity pocket account for the activation. The conformation of the P+1 pocket is similar to a second proline-directed kinase, CDK2-CyclinA, thus permitting the origin of this specificity to be defined. Conformational changes outside the lip provide loci at which the state of phosphorylation can be felt by other cellular components.
About this Structure
2ERK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation., Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ, Cell. 1997 Sep 5;90(5):859-69. PMID:9298898
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