Literature DB >> 1421163

Three-dimensional structure of p21H-ras and its implications.

F Wittinghofer1.   

Abstract

The three-dimensional structure of the H-ras oncogene product p21 has been determined in both its active, GTP-bound and its inactive, GDP-bound forms. This has supplied a wealth of information on the mode of binding of guanine nucleotides, on the mechanism of the GTPase reaction and on the conformational change of the protein which accompanies GTP hydrolysis. The structural analysis has also given clues to the interaction of p21 with the regulatory proteins GAP (GTPase Activating Protein) and nucleotide exchange factor. The three-dimensional structures of oncogenic mutants of p21 have also been determined and can nicely explain different biochemical and biological behaviour of these mutant proteins.

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Year:  1992        PMID: 1421163

Source DB:  PubMed          Journal:  Semin Cancer Biol        ISSN: 1044-579X            Impact factor:   15.707


  3 in total

1.  Molecular docking studies of protein-nucleotide complexes using MOLSDOCK (mutually orthogonal Latin squares DOCK).

Authors:  Shankaran Nehru Viji; Nagarajan Balaji; Namasivayam Gautham
Journal:  J Mol Model       Date:  2012-03-01       Impact factor: 1.810

2.  Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors.

Authors:  L A Quilliam; K Kato; K M Rabun; M M Hisaka; S Y Huff; S Campbell-Burk; C J Der
Journal:  Mol Cell Biol       Date:  1994-02       Impact factor: 4.272

3.  Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively regulates LET-60 Ras activity during vulval induction.

Authors:  T Gu; S Orita; M Han
Journal:  Mol Cell Biol       Date:  1998-08       Impact factor: 4.272

  3 in total

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