1uwh

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[[Image:1uwh.gif|left|200px]]
[[Image:1uwh.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1uwh |SIZE=350|CAPTION= <scene name='initialview01'>1uwh</scene>, resolution 2.95&Aring;
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The line below this paragraph, containing "STRUCTURE_1uwh", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BAX:4-{4-[({[4-CHLORO-3-(TRIFLUOROMETHYL)PHENYL]AMINO}CARBONYL)AMINO]PHENOXY}-N-METHYLPYRIDINE-2-CARBOXAMIDE'>BAX</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1uwh| PDB=1uwh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwh OCA], [http://www.ebi.ac.uk/pdbsum/1uwh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uwh RCSB]</span>
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}}
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'''THE COMPLEX OF WILD TYPE B-RAF AND BAY439006'''
'''THE COMPLEX OF WILD TYPE B-RAF AND BAY439006'''
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[[Category: Roe, S M.]]
[[Category: Roe, S M.]]
[[Category: Wan, P T.C.]]
[[Category: Wan, P T.C.]]
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[[Category: kinase]]
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[[Category: Kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:46:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:16:17 2008''
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Revision as of 08:46, 3 May 2008

Image:1uwh.gif


PDB ID 1uwh

Drag the structure with the mouse to rotate
1uwh, resolution 2.95Å ()
Ligands: ,
Related: 1uwj
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



THE COMPLEX OF WILD TYPE B-RAF AND BAY439006


Overview

Over 30 mutations of the B-RAF gene associated with human cancers have been identified, the majority of which are located within the kinase domain. Here we show that of 22 B-RAF mutants analyzed, 18 have elevated kinase activity and signal to ERK in vivo. Surprisingly, three mutants have reduced kinase activity towards MEK in vitro but, by activating C-RAF in vivo, signal to ERK in cells. The structures of wild type and oncogenic V599EB-RAF kinase domains in complex with the RAF inhibitor BAY43-9006 show that the activation segment is held in an inactive conformation by association with the P loop. The clustering of most mutations to these two regions suggests that disruption of this interaction converts B-RAF into its active conformation. The high activity mutants signal to ERK by directly phosphorylating MEK, whereas the impaired activity mutants stimulate MEK by activating endogenous C-RAF, possibly via an allosteric or transphosphorylation mechanism.

About this Structure

1UWH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF., Wan PT, Garnett MJ, Roe SM, Lee S, Niculescu-Duvaz D, Good VM, Jones CM, Marshall CJ, Springer CJ, Barford D, Marais R, Cell. 2004 Mar 19;116(6):855-67. PMID:15035987 Page seeded by OCA on Sat May 3 11:46:39 2008

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