Mutants arginine

Fig. 12. Tryptic map of it-PA (mol wt = 66,000) showing peptides formed from hydrolysis of reduced, alkylated rt-PA. Separation by reversed-phase octadecyl (C g) column using aqueous acetonitrile with an added acidic agent to the mobile phase. Arrows show the difference between A, normal, and B, mutant rt-PA where the glutamic acid residue, D, has replaced the normal arginine residue, C, at position 275.

Fig. 15. H-Ras mGTP shows a transient increase in fluorescence signal when mixed with the catalytic domain of the Ras-GAP neurofibromin (NF1). When wildtype NF1 is applied (gray trace) a decrease in signal follows, indicating the hydrolysis of mant-GTP. A NF1 mutant bearing an alanine at the position of the catalytic arginine residue (black trace) can only bind to Ras mant-GTP (increase) but cannot induce mant-GTP hydrolysis (no decrease). Figure kindly committed by Reza Ahmadian...

Analysis of the site-directed mutant proteins showed that the two arginine residues Arg359 and Arg528 are involved in the binding of the phosphate group of the acceptor compound. Asp477 (Fig. 2.2.2.1) is in close contact with the a-hy-... 

In the PI position, as expected, a basic group is preferred. Interestingly, of the two naturally occuring basic amino acids, arginine is preferred over lysine. This is seen in both the BPTI mutants as well as the... 

Shi, W. Sports, C.D. Raman, D. Shirakawa, S. Osawa, S. Weiss, E.R. Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal. Biochemistry, 37, 4869-4874 (1998)... 

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