1wnt
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1wnt.gif|left|200px]] | [[Image:1wnt.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1wnt", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{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''' | ||
| Line 33: | Line 30: | ||
[[Category: 6 alpha helice]] | [[Category: 6 alpha helice]] | ||
[[Category: 7 stranded parallel beta sheet]] | [[Category: 7 stranded parallel beta sheet]] | ||
| - | [[Category: | + | [[Category: Dinucleotide co-enzyme binding motif]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 10:55, 3 May 2008
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.
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 May 3 13:55:37 2008
