NMR Structure and Mutagenesis of the N-Terminal Dbl Homology Domain of the Nucleotide Exchange Factor Trio
In: Cell, Jg. 95 (1998-10-01), S. 269-277
Online
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Zugriff:
Guanine nucleotide exchange factors for the Rho family of GTPases contain a Dbl homology (DH) domain responsible for catalysis and a pleckstrin homology (PH) domain whose function is unknown. Here we describe the solution structure of the N-terminal DH domain of Trio that catalyzes nucleotide exchange for Rac1. The all-α-helical protein has a very different structure compared to other exchange factors. Based on site-directed mutagenesis, functionally important residues of the DH domain were identified. They are all highly conserved and reside in close proximity on two α helices. In addition, we have discovered a unique capability of the PH domain to enhance nucleotide exchange in DH domain–containing proteins.
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NMR Structure and Mutagenesis of the N-Terminal Dbl Homology Domain of the Nucleotide Exchange Factor Trio
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Autor/in / Beteiligte Person: | Jeff M Schkeryantz ; Olejniczak, Edward T. ; Eberstadt, Matthias ; Harris, Edith A. S. ; Fesik, Stephen W. ; Wang, Hong ; Liu, Xiaohong ; Meadows, Robert P. ; Janowick, David A. ; Staunton, Donald E. ; Schnuchel, Arndt ; Harlan, John E. |
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Zeitschrift: | Cell, Jg. 95 (1998-10-01), S. 269-277 |
Veröffentlichung: | Elsevier BV, 1998 |
Medientyp: | unknown |
ISSN: | 0092-8674 (print) |
DOI: | 10.1016/s0092-8674(00)81757-2 |
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