1frb: Difference between revisions

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New page: left|200px<br /><applet load="1frb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frb, resolution 1.7Å" /> '''FR-1 PROTEIN/NADPH/ZO...
 
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[[Image:1frb.gif|left|200px]]<br /><applet load="1frb" size="450" color="white" frame="true" align="right" spinBox="true"
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'''FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX'''<br />


==Overview==
==FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX==
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)
<StructureSection load='1frb' size='340' side='right'caption='[[1frb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1frb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRB FirstGlance]. <br>
1FRB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAP and ZST as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRB OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZST:3,4-DIHYDRO-4-OXO-3-((5-TRIFLUOROMETHYL-2-BENZOTHIAZOLYL)METHYL)-1-PHTHALAZINE+ACETIC+ACID'>ZST</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frb OCA], [https://pdbe.org/1frb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frb RCSB], [https://www.ebi.ac.uk/pdbsum/1frb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frb ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7578036 7578036]
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALD2_MOUSE ALD2_MOUSE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1frb ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Quiocho FA]]
[[Category: Quiocho, F.A.]]
[[Category: Wilson DK]]
[[Category: Wilson, D.K.]]
[[Category: NAP]]
[[Category: ZST]]
[[Category: aldo-keto oxidoreductase (nadp)]]
[[Category: tim barrel]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:11:13 2007''

Latest revision as of 10:18, 7 February 2024

FR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEXFR-1 PROTEIN/NADPH/ZOPOLRESTAT COMPLEX

Structural highlights

1frb is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALD2_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1frb, resolution 1.70Å

Drag the structure with the mouse to rotate

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