View source for 5brl


==Crystal Structure of L124D STARD4==
<StructureSection load='5brl' size='340' side='right'caption='[[5brl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5brl]] 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=5BRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BRL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.003&#8491;</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=5brl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5brl OCA], [https://pdbe.org/5brl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5brl RCSB], [https://www.ebi.ac.uk/pdbsum/5brl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5brl ProSAT]</span></td></tr>
</table>
== Function ==
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The steroidogenic acute regulatory protein-related lipid transfer (START) domain family is defined by a conserved 210-amino acid sequence that folds into an alpha/beta helix-grip structure. Members of this protein family bind a variety of ligands, including cholesterol, phospholipids, sphingolipids, and bile acids, with putative roles in nonvesicular lipid transport, metabolism, and cell signaling. Among the soluble START proteins, STARD4 is expressed in most tissues and has previously been shown to transfer sterol, but the molecular mechanisms of membrane interaction and sterol binding remain unclear. In this work, we use biochemical techniques to characterize regions of STARD4 and determine their role in membrane interaction and sterol binding. Our results show that STARD4 interacts with anionic membranes through a surface-exposed basic patch and that introducing a mutation (L124D) into the Omega-1 (Omega1) loop, which covers the sterol binding pocket, attenuates sterol transfer activity. To gain insight into the attenuating mechanism of the L124D mutation, we conducted structural and biophysical studies of wild-type and L124D STARD4. These studies show that the L124D mutation reduces the conformational flexibility of the protein, resulting in a diminished level of membrane interaction and sterol transfer. These studies also reveal that the C-terminal alpha-helix, and not the Omega1 loop, partitions into the membrane bilayer. On the basis of these observations, we propose a model of STARD4 membrane interaction and sterol binding and release that requires dynamic movement of both the Omega1 loop and membrane insertion of the C-terminal alpha-helix.

STARD4 Membrane Interactions and Sterol Binding.,Iaea DB, Dikiy I, Kiburu I, Eliezer D, Maxfield FR Biochemistry. 2015 Jul 22. PMID:26168008<ref>PMID:26168008</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5brl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Dikiy I]]
[[Category: Eliezer DE]]
[[Category: Iaea DB]]
[[Category: Kiburu I]]
[[Category: Maxfield FR]]