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.


1frb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1frb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1frb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1frb| PDB=1frb | SCENE= }}
{{STRUCTURE_1frb| PDB=1frb | SCENE= }}
-
'''FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX'''
+
===FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX===
-
==Overview==
+
<!--
-
Murine FR-1 is a protein that is induced by fibroblast growth factor-1 and, therefore, may play a role in the regulation of the cell cycle. Sequence comparison indicates that it is a member of the NADPH-dependent aldo-keto reductase family. It bears 70% identity to human aldose reductase, an enzyme implicated in diabetic complications and a target for drug design. We have determined the 1.7 A resolution structure of the FR-1 in a ternary complex with NADPH and zopolrestat, a potent aldose reductase inhibitor. FR-1 folds into a (beta/alpha)8 barrel with an active site characterized by a preponderance of hydrophobic residues residing in a deep oblong cavity at the C-terminal end of the beta-barrel. The nicotinamide moiety of the coenzyme sits in the base of the cavity. Zopolrestat occupies the active site cavity and makes numerous contacts with several hydrophobic residues. The FR-1 ternary complex structure indicates that it uses the same general catalytic mechanism as aldose reductase and other members of the family whose structures have been determined. The protein exhibits reductase activity with DL-glyceraldehyde as a substrate and is strongly inhibited by zopolrestat. When compared with the structure of a similar ternary complex of aldose reductase, the binding site retains many of the interactions with the coenzyme and inhibitor from the conserved residues. Some differences in sequence, however, create a larger binding site that contains six more water molecules than in the aldose reductase ternary complex structure.(ABSTRACT TRUNCATED AT 250 WORDS)
+
The line below this paragraph, {{ABSTRACT_PUBMED_7578036}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7578036 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7578036}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:40:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:49:39 2008''

Revision as of 00:49, 1 July 2008

Image:1frb.png

Template:STRUCTURE 1frb

FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX

Template:ABSTRACT PUBMED 7578036

About this Structure

1FRB is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor., Wilson DK, Nakano T, Petrash JM, Quiocho FA, Biochemistry. 1995 Nov 7;34(44):14323-30. PMID:7578036

Page seeded by OCA on Tue Jul 1 03:49:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1frb"
Personal tools