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.


1llg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1llg" [edit=sysop:move=sysop])
Current revision (06:46, 18 August 2021) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
{{Theoretical_model}}
{{Theoretical_model}}
-
[[Image:1llg.png|left|200px]]
+
==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 [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'>[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>
 +
<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.
-
{{STRUCTURE_1llg| PDB=1llg | SCENE= }}
+
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>
-
===HOMOLOGY MODELLING OF RHO-CRYSTALLIN FROM BULL FROG (RANA CATESBEIANA) LENS===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_15177080}}
+
<div class="pdbe-citations 1llg" style="background-color:#fffaf0;"></div>
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:015177080</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
 +
[[Category: Theoretical Model]]
 +
[[Category: Large Structures]]
[[Category: Zaidi, Z H]]
[[Category: Zaidi, Z H]]
[[Category: Zarina, S]]
[[Category: Zarina, S]]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools