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.

4jih

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 18:03, 5 August 2016

Crystal Structure Of AKR1B10 Complexed With NADP+ And Epalrestat

Structural highlights

4jih is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	4jii, 4jir, 4gqg, 4gq0, 4i5x
Gene:	AKR1B10, AKR1B11 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AK1BA_HUMAN] Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs.^[1]

Publication Abstract from PubMed

The antineoplastic target aldo-keto reductase family member 1B10 (AKR1B10) and the critical polyol pathway enzyme aldose reductase (AKR1B1) share high structural similarity. Crystal structures reported here reveal a surprising Trp112 native conformation stabilized by a specific Gln114-centered hydrogen bond network in the AKR1B10 holoenzyme, and suggest that AKR1B1 inhibitors could retain their binding affinities toward AKR1B10 by inducing Trp112 flip to result in an "AKR1B1-like" active site in AKR1B10, while selective AKR1B10 inhibitors can take advantage of the broader active site of AKR1B10 provided by the native Trp112 side-chain orientation.

Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111).,Zhang L, Zhang H, Zhao Y, Li Z, Chen S, Zhai J, Chen Y, Xie W, Wang Z, Li Q, Zheng X, Hu X FEBS Lett. 2013 Oct 4. pii: S0014-5793(13)00726-6. doi:, 10.1016/j.febslet.2013.09.031. PMID:24100137^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gallego O, Ruiz FX, Ardevol A, Dominguez M, Alvarez R, de Lera AR, Rovira C, Farres J, Fita I, Pares X. Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc Natl Acad Sci U S A. 2007 Dec 26;104(52):20764-9. Epub 2007 Dec 17. PMID:18087047
↑ Zhang L, Zhang H, Zhao Y, Li Z, Chen S, Zhai J, Chen Y, Xie W, Wang Z, Li Q, Zheng X, Hu X. Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111). FEBS Lett. 2013 Oct 4. pii: S0014-5793(13)00726-6. doi:, 10.1016/j.febslet.2013.09.031. PMID:24100137 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.031

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4jih"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Of AKR1B10 Complexed With NADP+ And Epalrestat==
 <StructureSection load='4jih' size='340' side='right' caption='[[4jih]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jii|4jii]], [[4jir|4jir]], [[4gqg|4gqg]], [[4gq0|4gq0]], [[4i5x|4i5x]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKR1B10, AKR1B11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jih RCSB], [http://www.ebi.ac.uk/pdbsum/4jih PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jih OCA], [http://pdbe.org/4jih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jih RCSB], [http://www.ebi.ac.uk/pdbsum/4jih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jih ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4jih" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4jih

From Proteopedia

Revision as of 18:03, 5 August 2016

Crystal Structure Of AKR1B10 Complexed With NADP+ And Epalrestat

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox