1o5w
From Proteopedia
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|PDB= 1o5w |SIZE=350|CAPTION= <scene name='initialview01'>1o5w</scene>, resolution 3.20Å | |PDB= 1o5w |SIZE=350|CAPTION= <scene name='initialview01'>1o5w</scene>, resolution 3.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MLG:N-[3-(2,4-DICHLOROPHENOXY)PROPYL]-N-METHYL-N-PROP-2-YNYLAMINE'>MLG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o5w OCA], [http://www.ebi.ac.uk/pdbsum/1o5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o5w RCSB]</span> | ||
}} | }} | ||
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[[Category: Yamashita, E.]] | [[Category: Yamashita, E.]] | ||
[[Category: Yoshimura, M.]] | [[Category: Yoshimura, M.]] | ||
| - | [[Category: FAD]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:16 2008'' |
Revision as of 19:40, 30 March 2008
| |||||||
| , resolution 3.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Amine oxidase (flavin-containing), with EC number 1.4.3.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structure basis of specific recognitions for substrates and inhibitors of rat monoamine oxidase A
Overview
Monoamine oxidase (MAO), a mitochondrial outer membrane enzyme, catalyzes the degradation of neurotransmitters in the central nervous system and is the target for anti-depression drug design. Two subtypes of MAO, MAOA and MAOB, are similar in primary sequences but have unique substrate and inhibitor specificities. The structures of human MAOB complexed with various inhibitors were reported early. To understand the mechanisms of specific substrate and inhibitor recognitions of MAOA and MAOB, we have determined the crystal structure of rat MAOA complexed with the specific inhibitor, clorgyline, at 3.2A resolution. The comparison of the structures between MAOA and MAOB clearly explains the specificity of clorgyline for MAOA inhibition. The fitting of serotonin into the binding pockets of MAOs demonstrates that MAOB Tyr326 would block access of the 5-hydroxy group of serotonin into the enzyme. These results will lead to further understanding of the MAOA function and to new anti-depression drug design. This study also presents that MAOA has a transmembrane helix at the C-terminal region. This is the first crystal structure of membrane protein with an isolated transmembrane helix.
About this Structure
1O5W is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors., Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, Tsukihara T, J Mol Biol. 2004 Apr 16;338(1):103-14. PMID:15050826
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