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  Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras

Scheffzek, K., Lautwein, A., Kabsch, W., Ahmadian, M. R., & Wittinghofer, A. (1996). Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature, 384, 591-596.

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Genre: Journal Article
Alternative Title : Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras

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Nature_384_1996_591.pdf (Any fulltext), 2MB
 
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Scheffzek, Klaus1, Author              
Lautwein, Alfred, Author
Kabsch, Wolfgang1, Author              
Ahmadian, Mohammad Reza, Author
Wittinghofer, Alfred1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Ras-related GTP-binding proteins function as molecular switches which cycle between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common timing mechanism that mediates the return from the 'on' to the 'off'-state. It is usually slow but can be accelerated by orders of magnitude upon interaction with GTPase-activating proteins (GAPs). In the case of Ras, a major regulator of cellular growth, point mutations are found in approximately 30% of human tumours which render the protein unable to hydrolyse GTP, even in the presence of Ras-GAPs. The first structure determination of a GTPase-activating protein reveals the catalytically active fragment of the Ras-specific p120GAP (ref. 2), GAP-334, as an elongated, exclusively helical protein which appears to represent a novel protein fold. The molecule consists of two domains, one of which contains all the residues conserved among different GAPs for Ras. From the location of conserved residues around a shallow groove in the central domain we can identify the site of interaction with Ras x GTP. This leads to a model for the interaction between Ras and GAP that satisfies numerous biochemical and genetic data on this important regulatory process

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Language(s): eng - English
 Dates: 1996-09-101996-11-191996
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666430
Other: 4577
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Title: Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 384 Sequence Number: - Start / End Page: 591 - 596 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238