1llg: Difference between revisions

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