1xgg: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1xgg.png|left|200px]]
-<!--
+==THEORETICAL MODEL OF THE CELLULAR RETINALDEHYDE BINDING PROTEIN IN ITS CLOSED CONFORMATION==
-The line below this paragraph, containing "STRUCTURE_1xgg", creates the "Structure Box" on the page.
+<StructureSection load='1xgg' size='340' side='right'caption='[[1xgg]]' 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=1XGG 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=1xgg FirstGlance], [https://www.ebi.ac.uk/pdbsum/1xgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgg ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1xgg|  PDB=1xgg  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cellular retinaldehyde-binding protein (CRALBP) is an essential protein in the human visual cycle without a known three-dimensional structure. Previous studies associate retinal pathologies to specific mutations in the CRALBP protein. Here we use homology modeling and molecular dynamics methods to investigate the structural mechanisms by which CRALBP functions in the visual cycle. We have constructed two conformations of CRALBP representing two states in the process of ligand association and dissociation. Notably, our homology models map the pathology-associated mutations either directly in or adjacent to the putative ligand-binding cavity. Furthermore, six novel residues have been identified to be crucial for the hinge movement of the lipid-exchange loop in CRALBP. We conclude that the binding and release of retinoid involve large conformational changes in the lipid-exchange loop at the entrance of the ligand-binding cavity.
-===THEORETICAL MODEL OF THE CELLULAR RETINALDEHYDE BINDING PROTEIN IN ITS CLOSED CONFORMATION===
+Structural insights into the cellular retinaldehyde-binding protein (CRALBP).,Liu T, Jenwitheesuk E, Teller DC, Samudrala R Proteins. 2005 Nov 1;61(2):412-22. PMID:16121400<ref>PMID:16121400</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_16121400}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1xgg" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16121400 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16121400}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGG OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:16121400</ref><references group="xtra"/>
 [[Category: Jenwitheesuk, E]]
 [[Category: Liu, T]]
 [[Category: Samudrala, R]]
 [[Category: Teller, D C]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:21:56 2010''