1llg

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1llg.png|left|200px]]
 
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==HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS==
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The line below this paragraph, containing "STRUCTURE_1llg", creates the "Structure Box" on the page.
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<StructureSection load='1llg' size='340' side='right'caption='[[1llg]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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</table>
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{{STRUCTURE_1llg| PDB=1llg | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15177080}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1llg" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15177080 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15177080}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLG OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:15177080</ref><references group="xtra"/>
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[[Category: Zaidi, Z H]]
[[Category: Zaidi, Z H]]
[[Category: Zarina, S]]
[[Category: Zarina, S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:05:06 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS

PDB ID 1llg

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