1mt5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1mt5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mt5, resolution 2.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1mt5.gif|left|200px]]<br /><applet load="1mt5" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1mt5.gif|left|200px]]<br /><applet load="1mt5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mt5, resolution 2.80&Aring;" />
caption="1mt5, resolution 2.80&Aring;" />
'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''<br />
'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1MT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MAY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MT5 OCA].
+
1MT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MAY:'>MAY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT5 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Bracey, M.H.]]
+
[[Category: Bracey, M H.]]
-
[[Category: Cravatt, B.F.]]
+
[[Category: Cravatt, B F.]]
-
[[Category: Hanson, M.A.]]
+
[[Category: Hanson, M A.]]
-
[[Category: Masuda, K.R.]]
+
[[Category: Masuda, K R.]]
-
[[Category: Stevens, R.C.]]
+
[[Category: Stevens, R C.]]
[[Category: MAY]]
[[Category: MAY]]
[[Category: amidase signature]]
[[Category: amidase signature]]
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:40:49 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:47 2008''

Revision as of 11:58, 21 February 2008


1mt5, resolution 2.80Å

Drag the structure with the mouse to rotate

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 with as ligand. 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 Thu Feb 21 13:58:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools