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Team Of Max Planck Scientists Elucidates Structure Of A Protein Segment Involved In 'Von Recklinghausen Neurofibromatosis'

1261-1268). Since this mutation was the only one found in the whole NF1 gene of the respective patient, it appears that loss of GAP function is sufficient for the development of neurofibromatosis.

The medical impact of the work on neurofibromin and p120GAP is twofold: on the one hand it is now possible to picture how neurofibromin acts on Ras and to analyze mutations in the light of the structure; on the other hand, the structure of the contact area between GAP and Ras suggests that it might be attractive to search for small molecules that may act as surrogate GAPs in tumor cells where Ras is fatally mutated or its GTP-bound levels are increased for other reasons, e.g. due to a missing neurofibromin function. The 3-dimensional picture of GAP and of its communication with Ras may suggest how to proceed, but also indicates us that it will be an extremely formidable task.


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Contact: Klaus Scheffzek
Klaus.Scheffzek@mpi-dortmund.mpg.de
Fax: 49-231-1206-23
Max-Planck-Gesellschaft
14-Aug-1998


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