This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.




2byb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2byb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2byb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2byb| PDB=2byb | SCENE= }}
{{STRUCTURE_2byb| PDB=2byb | SCENE= }}
-
'''HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL'''
+
===HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL===
-
==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 34: Line 38:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Transmembrane neurotransmitter]]
[[Category: Transmembrane neurotransmitter]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:37:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:20:02 2008''

Revision as of 18:20, 28 July 2008

Template:STRUCTURE 2byb

HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH DEPRENYL

Template:ABSTRACT PUBMED 16129825

About this Structure

2BYB 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 Mon Jul 28 21:20:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools