1jss

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<StructureSection load='1jss' size='340' side='right'caption='[[1jss]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1jss' size='340' side='right'caption='[[1jss]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1jss]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JSS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1jss]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JSS FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC005642; Unigene Cluster: Mm. 31508 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jss OCA], [http://pdbe.org/1jss PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jss RCSB], [http://www.ebi.ac.uk/pdbsum/1jss PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jss ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1jss TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jss OCA], [https://pdbe.org/1jss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jss RCSB], [https://www.ebi.ac.uk/pdbsum/1jss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jss ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1jss TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/STAR4_MOUSE STAR4_MOUSE]] May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols.
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[https://www.uniprot.org/uniprot/STAR4_MOUSE STAR4_MOUSE] May be involved in the intracellular transport of sterols or other lipids. May bind cholesterol or other sterols.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jss ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jss ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64. The volume of the putative lipid-binding tunnel was estimated at 847 A(3), which is consistent with the binding of one cholesterol-size lipid molecule. Comparison of the tunnel-lining residues in StarD4 and MLN64-START permitted identification of possible lipid specificity determinants in both molecular tunnels. Homology modeling of related proteins, and comparison of the StarD4 and MLN64-START structures, showed that StarD4 is a member of a large START domain superfamily characterized by the helix-grip fold. Additional mechanistic and evolutionary studies should be facilitated by the availability of a second START domain structure from a distant relative of MLN64.
 
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Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain.,Romanowski MJ, Soccio RE, Breslow JL, Burley SK Proc Natl Acad Sci U S A. 2002 May 14;99(10):6949-54. PMID:12011453<ref>PMID:12011453</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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<div class="pdbe-citations 1jss" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Breslow, J L]]
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[[Category: Breslow JL]]
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[[Category: Burley, S K]]
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[[Category: Burley SK]]
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[[Category: Structural genomic]]
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[[Category: Romanowski MJ]]
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[[Category: Romanowski, M J]]
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[[Category: Soccio RE]]
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[[Category: Soccio, R E]]
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[[Category: Lipid binding protein]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Start domain]]
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Revision as of 07:42, 7 February 2024

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).

PDB ID 1jss

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