1pq3: Difference between revisions

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[[Image:1pq3.jpg|left|200px]]
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{{STRUCTURE_1pq3|  PDB=1pq3  |  SCENE=  }}  
{{STRUCTURE_1pq3|  PDB=1pq3  |  SCENE=  }}  


'''Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal'''
===Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal===




==Overview==
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Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. The X-ray crystal structure of a fully active, truncated form of human arginase II complexed with a boronic acid transition state analogue inhibitor has been determined at 2.7 A resolution. This structure is consistent with the hydrolysis of l-arginine through a metal-activated hydroxide mechanism. Given that human arginase II appears to play a role in regulating l-arginine bioavailability to NO synthase in human penile corpus cavernosum smooth muscle, the inhibition of human arginase II is a potential new strategy for the treatment of erectile dysfunction [Kim, N. N., Cox, J. D., Baggio, R. F., Emig, F. A., Mistry, S., Harper, S. L., Speicher, D. W., Morris, S. M., Ash, D. E., Traish, A. M., and Christianson, D. W. (2001) Biochemistry 40, 2678-2688]. Since NO synthase is found in human clitoral corpus cavernosum and vagina, we hypothesized that human arginase II is similarly present in these tissues and functions to regulate l-arginine bioavailability to NO synthase. Accordingly, hemodynamic studies conducted with a boronic acid arginase inhibitor in vivo are summarized, suggesting that the extrahepatic arginase plays a role in both male and female sexual arousal. Therefore, arginase II is a potential target for the treatment of male and female sexual arousal disorders.
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==About this Structure==
==About this Structure==
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[[Category: Traish, A M.]]
[[Category: Traish, A M.]]
[[Category: Biosynthetic protein]]
[[Category: Biosynthetic protein]]
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