1mt5

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[[Image:1mt5.gif|left|200px]]
[[Image:1mt5.gif|left|200px]]
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{{Structure
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|PDB= 1mt5 |SIZE=350|CAPTION= <scene name='initialview01'>1mt5</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1mt5", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MAY:METHYL+ARACHIDONYL+FLUOROPHOSPHONATE'>MAY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= FAAH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=
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{{STRUCTURE_1mt5| PDB=1mt5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt5 OCA], [http://www.ebi.ac.uk/pdbsum/1mt5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mt5 RCSB]</span>
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'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''
'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''
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[[Category: Masuda, K R.]]
[[Category: Masuda, K R.]]
[[Category: Stevens, R C.]]
[[Category: Stevens, R C.]]
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[[Category: amidase signature]]
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[[Category: Amidase signature]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:41:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:51 2008''
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Revision as of 22:41, 2 May 2008

Template:STRUCTURE 1mt5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE


Overview

Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.

About this Structure

1MT5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling., Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF, Science. 2002 Nov 29;298(5599):1793-6. PMID:12459591 Page seeded by OCA on Sat May 3 01:41:19 2008

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