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2e14

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[[Image:2e14.jpg|left|200px]]<br /><applet load="2e14" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2e14.jpg|left|200px]]
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caption="2e14, resolution 3.0&Aring;" />
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'''The structure of ERK2 in complex with FR148083'''<br />
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{{Structure
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|PDB= 2e14 |SIZE=350|CAPTION= <scene name='initialview01'>2e14</scene>, resolution 3.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FRR:(3R,5Z,8S,9S,11E)-8,9,16-TRIHYDROXY-14-METHOXY-3-METHYL-3,4,9,10-TETRAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,7(8H)-DIONE'>FRR</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase Mitogen-activated protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.24 2.7.11.24]
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|GENE=
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}}
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'''The structure of ERK2 in complex with FR148083'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2E14 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FRR:'>FRR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase Mitogen-activated protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.24 2.7.11.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E14 OCA].
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2E14 is a [[Single protein]] 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=2E14 OCA].
==Reference==
==Reference==
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Role of a cysteine residue in the active site of ERK and the MAPKK family., Ohori M, Kinoshita T, Yoshimura S, Warizaya M, Nakajima H, Miyake H, Biochem Biophys Res Commun. 2007 Feb 16;353(3):633-7. Epub 2006 Dec 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17194451 17194451]
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Role of a cysteine residue in the active site of ERK and the MAPKK family., Ohori M, Kinoshita T, Yoshimura S, Warizaya M, Nakajima H, Miyake H, Biochem Biophys Res Commun. 2007 Feb 16;353(3):633-7. Epub 2006 Dec 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17194451 17194451]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mitogen-activated protein kinase]]
[[Category: Mitogen-activated protein kinase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:33:54 2008''

Revision as of 14:33, 20 March 2008


PDB ID 2e14

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands:
Activity: Mitogen-activated protein kinase, with EC number 2.7.11.24
Coordinates: save as pdb, mmCIF, xml



The structure of ERK2 in complex with FR148083


Contents

Overview

Kinases of mitogen-activated protein kinase (MAPK) cascades, including extracellular signal-regulated protein kinase (ERK), represent likely targets for pharmacological intervention in proliferative diseases. Here, we report that FR148083 inhibits ERK2 enzyme activity and TGFbeta-induced AP-1-dependent luciferase expression with respective IC50 values of 0.08 and 0.05 microM. FR265083 (1'-2' dihydro form) and FR263574 (1'-2' and 7'-8' tetrahydro form) exhibited 5.5-fold less and no activity, respectively, indicating that both the alpha,beta-unsaturated ketone and the conformation of the lactone ring contribute to this inhibitory activity. The X-ray crystal structure of the ERK2/FR148083 complex revealed that the compound binds to the ATP binding site of ERK2, involving a covalent bond to Sgamma of ERK2 Cys166, hydrogen bonds with the backbone NH of Met108, Nzeta of Lys114, backbone C=O of Ser153, Ndelta2 of Asn154, and hydrophobic interactions with the side chains of Ile31, Val39, Ala52, and Leu156. The covalent bond motif in the ERK2/FR148083 complex assures that the inhibitor has high activity for ERK2 and no activity for other MAPKs such as JNK1 and p38MAPKalpha/beta/gamma/delta which have leucine residues at the site corresponding to Cys166 in ERK2. On the other hand, MEK1 and MKK7, kinases of the MAPKK family which also can be inhibited by FR148083, contain a cysteine residue corresponding to Cys166 of ERK2. The covalent binding to the common cysteine residue in the ATP-binding site is therefore likely to play a crucial role in the inhibitory activity for these MAP kinases. These findings on the molecular recognition mechanisms of FR148083 for kinases with Cys166 should provide a novel strategy for the pharmacological intervention of MAPK cascades.

Disease

Known diseases associated with this structure: Epileptic encephalopathy, Lennox-Gastaut type OMIM:[602897]

About this Structure

2E14 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Role of a cysteine residue in the active site of ERK and the MAPKK family., Ohori M, Kinoshita T, Yoshimura S, Warizaya M, Nakajima H, Miyake H, Biochem Biophys Res Commun. 2007 Feb 16;353(3):633-7. Epub 2006 Dec 20. PMID:17194451

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