1pq3
From Proteopedia
(New page: 200px<br /> <applet load="1pq3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pq3, resolution 2.70Å" /> '''Human Arginase II: ...) |
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caption="1pq3, resolution 2.70Å" /> | caption="1pq3, resolution 2.70Å" /> | ||
'''Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal'''<br /> | '''Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4, MN, CL and S2C as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http:// | + | 1PQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=S2C:'>S2C</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQ3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: biosynthetic protein]] | [[Category: biosynthetic protein]] | ||
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Revision as of 14:41, 15 February 2008
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Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal
Overview
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.
About this Structure
1PQ3 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Arginase, with EC number 3.5.3.1 Full crystallographic information is available from OCA.
Reference
Human arginase II: crystal structure and physiological role in male and female sexual arousal., Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW, Biochemistry. 2003 Jul 22;42(28):8445-51. PMID:12859189
Page seeded by OCA on Fri Feb 15 16:40:59 2008
Categories: Arginase | Homo sapiens | Single protein | Ash, D.E. | Cama, E. | Christianson, D.W. | Colleluori, D.M. | Emig, F.A. | Kim, N.N. | Kim, S.W. | Shin, H. | Traish, A.M. | CL | MN | S2C | SO4 | Biosynthetic protein
