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| - | ==STRUCTURE OF SIGNAL-REGULATED KINASE==
| + | #REDIRECT [[5umo]] This PDB entry is obsolete and replaced by 5umo |
| - | <StructureSection load='1erk' size='340' side='right' caption='[[1erk]], [[Resolution|resolution]] 2.30Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1erk]] is a 1 chain structure 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=1ERK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ERK FirstGlance]. <br>
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| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1erk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1erk RCSB], [http://www.ebi.ac.uk/pdbsum/1erk PDBsum]</span></td></tr>
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| - | </table>
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| - | == Evolutionary Conservation ==
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| - | [[Image:Consurf_key_small.gif|200px|right]]
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| - | Check<jmol>
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| - | <jmolCheckbox>
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| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/1erk_consurf.spt"</scriptWhenChecked>
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| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| - | <text>to colour the structure by Evolutionary Conservation</text>
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| - | </jmolCheckbox>
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| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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| - | <div style="clear:both"></div>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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<ref>PMID:8107865</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | ==See Also==
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| - | *[[Mitogen-activated protein kinase|Mitogen-activated protein kinase]]
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Rattus norvegicus]]
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| - | [[Category: Goldsmith, E J]]
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| - | [[Category: Harkins, P C]]
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| - | [[Category: Atp-binding cell cycle]]
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| - | [[Category: Phosphorylation]]
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| - | [[Category: Serine/threonine-protein kinase]]
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| - | [[Category: Transferase]]
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