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==HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS== | |||
<StructureSection load='1llg' size='340' side='right' caption='[[1llg]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LLG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1llg FirstGlance], [http://www.ebi.ac.uk/pdbsum/1llg PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
rho-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<ref>PMID:15177080</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Zaidi, Z H]] | [[Category: Zaidi, Z H]] | ||
[[Category: Zarina, S]] | [[Category: Zarina, S]] | ||
Revision as of 18:27, 28 September 2014
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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