1jss

<StructureSection load='1jss' size='340' side='right' caption='[[1jss]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JSS FirstGlance]. <br>

</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>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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://www.topsan.org/Proteins/NYSGXRC/1jss TOPSAN]</span></td></tr>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/1jss_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jss" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Breslow, J L]]

[[Category: Burley, S K]]

[[Category: Structural genomic]]

[[Category: Romanowski, M J]]

[[Category: Soccio, R E]]

[[Category: Start domain]]