1llg: Difference between revisions
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==HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS== | ==HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS== | ||
<StructureSection load='1llg' size='340' side='right' caption='[[1llg]]' scene=''> | <StructureSection load='1llg' size='340' side='right'caption='[[1llg]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLG FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1llg FirstGlance], [https://www.ebi.ac.uk/pdbsum/1llg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Theoretical Model]] | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
[[Category: Zaidi, Z H]] | [[Category: Zaidi, Z H]] | ||
[[Category: Zarina, S]] | [[Category: Zarina, S]] | ||
Latest revision as of 09:46, 18 August 2021
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HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENSHOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS
Structural highlights
Publication Abstract from PubMedrho-Crystallins are major protein component found in the eye lenses of frogs of the genus Rana. Structural analysis has indicated that frog rho-crystallins belong to aldo-keto reductase superfamily (AKRs) which include aldehyde and aldose reductases, prostaglandin F synthase and several detoxification enzymes. Members of AKRs catalyze the oxidation-reduction reaction over a range of substrates using NAD(P)(H) as a cofactor. In spite of higher structural similarity with AKRs and cofactor binding affinity, the rho-crystallins were found to be catalytically inactive. This study presents comparative or homology modeling of rho-crystallin from bullfrog (Rana catesbeiana) in presence and absence of cofactor NADP and a competitive inhibitor, testosterone. The predicted models are explored to examine the catalytic cleft, cofactor binding affinity characteristics and substrate binding pocket. Homology modeling of rho-crystallin from bullfrog (Rana catesbeiana) lens.,Zarina S, Zaidi ZH J Mol Graph Model. 2004 Mar;22(4):285-91. PMID:15177080[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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