1wnt: 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:1wnt.gif|left|200px]]
{{Seed}}
[[Image:1wnt.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wnt|  PDB=1wnt  |  SCENE=  }}  
{{STRUCTURE_1wnt|  PDB=1wnt  |  SCENE=  }}  


'''Strucutre of the tetrameric form of Human L-Xylulose Reductase'''
===Strucutre of the tetrameric form of Human L-Xylulose Reductase===




==Overview==
<!--  
L-Xylulose reductase (XR) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. In this study we report the structure of the biological tetramer of human XR in complex with NADP(+) and a competitive inhibitor solved at 2.3 A resolution. A single subunit of human XR is formed by a centrally positioned, seven-stranded, parallel beta-sheet surrounded on either side by two arrays of three alpha-helices. Two helices located away from the main body of the protein form the variable substrate-binding cleft, while the dinucleotide coenzyme-binding motif is formed by a classical Rossmann fold. The tetrameric structure of XR, which is held together via salt bridges formed by the guanidino group of Arg203 from one monomer and the carboxylate group of the C-terminal residue Cys244 from the neighboring monomer, explains the ability of human XR to prevent the cold inactivation seen in the rodent forms of the enzyme. The orientations of Arg203 and Cys244 are maintained by a network of hydrogen bonds and main-chain interactions of Gln137, Glu238, Phe241, and Trp242. These interactions are similar to those defining the quaternary structure of the closely related carbonyl reductase from mouse lung. Molecular modeling and site-directed mutagenesis identified the active site residues His146 and Trp191 as forming essential contacts with inhibitors of XR. These results could provide a structural basis in the design of potent and specific inhibitors for human XR.
The line below this paragraph, {{ABSTRACT_PUBMED_15906319}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15906319 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15906319}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Dinucleotide co-enzyme binding motif]]
[[Category: Dinucleotide co-enzyme binding motif]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:55:37 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:21:12 2008''

Revision as of 13:21, 5 July 2008

File:1wnt.png

Template:STRUCTURE 1wnt

Strucutre of the tetrameric form of Human L-Xylulose Reductase

Template:ABSTRACT PUBMED 15906319

About this Structure

1WNT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the tetrameric form of human L-Xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis., El-Kabbani O, Carbone V, Darmanin C, Ishikura S, Hara A, Proteins. 2005 Aug 15;60(3):424-32. PMID:15906319

Page seeded by OCA on Sat Jul 5 16:21:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1wnt&oldid=636616"