View source for 7dpx


==Crystal structure of the SRCR domain of human SCARA1/CD204==
<StructureSection load='7dpx' size='340' side='right'caption='[[7dpx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DPX 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]] 2.002&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=7dpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dpx OCA], [https://pdbe.org/7dpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dpx RCSB], [https://www.ebi.ac.uk/pdbsum/7dpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dpx ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Scavenger receptor class A (SR-A) proteins are type II transmembrane glycoproteins that form homotrimers on the cell surface. This family has five known members (SCARA1 to 5, or SR-A1 to A5) that recognize a variety of ligands and are involved in multiple biological pathways. Previous reports have shown that some SR-A family members can bind modified low-density lipoproteins (LDL); however, the mechanisms of the interactions between the SR-A members and these lipoproteins are not fully understood. Here we systematically characterize the recognition of SR-A receptors with lipoproteins and report that SCARA1 (SR-A1, CD204), MARCO (SCARA2), and SCARA5 recognize acetylated or oxidized LDL and very low-density lipoproteins (VLDL) in a Ca(2+)-dependent manner through their C-terminal scavenger receptor cysteine-rich (SRCR) domains. These interactions occur specifically between the SRCR domains and the modified apoB component of the lipoproteins, suggesting that they might share a similar mechanism for lipoprotein recognition. Meanwhile, SCARA4, a SR-A member with a carbohydrate recognition domain instead of the SRCR domain at the C-terminus, shows low affinity for modified LDL and VLDL, but binds in a Ca(2+)-independent manner. SCARA3, which does not have a globular domain at the C-terminus, was found to have no detectable binding with these lipoproteins. Taken together, these results provide mechanistic insights into the interactions between SR-A family members and lipoproteins that may help us to understand the roles of SR-A receptors in lipid transport and related diseases such as atherosclerosis.

Recognition of lipoproteins by scavenger receptor class A members.,Cheng C, Zheng E, Yu B, Zhang Z, Wang Y, Liu Y, He Y J Biol Chem. 2021 Jul 9:100948. doi: 10.1016/j.jbc.2021.100948. PMID:34252459<ref>PMID:34252459</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 7dpx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cheng C]]
[[Category: He Y]]