1uwj

Revision as of 18:05, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1uwj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uwj, resolution 3.50Å" /> '''THE COMPLEX OF MUTA...)
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THE COMPLEX OF MUTANT V599E B-RAF AND BAY439006

File:1uwj.gif


1uwj, resolution 3.50Å

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OverviewOverview

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 ... [(full description)]

About this StructureAbout this Structure

1UWJ is a [Single protein] structure of sequence from [Homo sapiens] with BAX as [ligand]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].

ReferenceReference

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

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