2bxr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2bxr.gif|left|200px]]
{{Seed}}
[[Image:2bxr.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bxr|  PDB=2bxr  |  SCENE=  }}  
{{STRUCTURE_2bxr|  PDB=2bxr  |  SCENE=  }}  


'''HUMAN MONOAMINE OXIDASE A IN COMPLEX WITH CLORGYLINE, CRYSTAL FORM A'''
===HUMAN MONOAMINE OXIDASE A IN COMPLEX WITH CLORGYLINE, CRYSTAL FORM A===




==Overview==
<!--
The three-dimensional structure of recombinant human monoamine oxidase A (hMAO A) as its clorgyline-inhibited adduct is described. Although the chain-fold of hMAO A is similar to that of rat MAO A and human MAO B (hMAO B), hMAO A is unique in that it crystallizes as a monomer and exhibits the solution hydrodynamic behavior of a monomeric form rather than the dimeric form of hMAO B and rat MAO A. hMAO A's active site consists of a single hydrophobic cavity of approximately 550 A3, which is smaller than that determined from the structure of deprenyl-inhibited hMAO B (approximately 700 A3) but larger than that of rat MAO A (approximately 450 A3). An important component of the active site structure of hMAO A is the loop conformation of residues 210-216, which differs from that of hMAO B and rat MAO A. The origin of this structural alteration is suggested to result from long-range interactions in the monomeric form of the enzyme. In addition to serving as a basis for the development of hMAO A specific inhibitors, these data support the proposal that hMAO A involves a change from the dimeric to the monomeric form through a Glu-151 --&gt; Lys mutation that is specific of hMAO A [Andres, A. M., Soldevila, M., Navarro, A., Kidd, K. K., Oliva, B. &amp; Bertranpetit, J. (2004) Hum. Genet. 115, 377-386]. These considerations put into question the use of MAO A from nonhuman sources in drug development for use in humans.
The line below this paragraph, {{ABSTRACT_PUBMED_16129825}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16129825 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16129825}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Neurotransmitter]]
[[Category: Neurotransmitter]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:37:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:13:05 2008''

Revision as of 10:13, 29 July 2008

File:2bxr.png

Template:STRUCTURE 2bxr

HUMAN MONOAMINE OXIDASE A IN COMPLEX WITH CLORGYLINE, CRYSTAL FORM A

Template:ABSTRACT PUBMED 16129825

About this Structure

2BXR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B., De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. PMID:16129825

Page seeded by OCA on Tue Jul 29 13:13:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2bxr&oldid=742671"