1mt5

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{{STRUCTURE_1mt5| PDB=1mt5 | SCENE= }}
{{STRUCTURE_1mt5| PDB=1mt5 | SCENE= }}
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'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''
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===CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12459591 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12459591}}
==About this Structure==
==About this Structure==
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[[Category: Amidase signature]]
[[Category: Amidase signature]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:37:04 2008''

Revision as of 05:37, 28 July 2008

Image:1mt5.png

Template:STRUCTURE 1mt5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

Template:ABSTRACT PUBMED 12459591

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 Mon Jul 28 08:37:04 2008

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