View source for 8hbc


==Crystal structure of the CysR-CTLD3 fragment of human DEC205==
<StructureSection load='8hbc' size='340' side='right'caption='[[8hbc]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HBC 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]] 3.35&#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=8hbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hbc OCA], [https://pdbe.org/8hbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hbc RCSB], [https://www.ebi.ac.uk/pdbsum/8hbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hbc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LY75_HUMAN LY75_HUMAN] Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment (By similarity). Causes reduced proliferation of B-lymphocytes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DEC205 (CD205) is one of the major endocytic receptors on dendritic cells and has been widely used as a receptor target in immune therapies. It has been shown that DEC205 can recognize dead cells through keratins in a pH-dependent manner. However, the mechanism underlying the interaction between DEC205 and keratins remains unclear. Here we determine the crystal structures of an N-terminal fragment of human DEC205 (CysR approximately CTLD3). The structural data show that DEC205 shares similar overall features with the other mannose receptor family members such as the mannose receptor and Endo180, but the individual domains of DEC205 in the crystal structure exhibit distinct structural features that may lead to specific ligand binding properties of the molecule. Among them, CTLD3 of DEC205 adopts a unique fold of CTLD, which may correlate with the binding of keratins. Furthermore, we examine the interaction of DEC205 with keratins by mutagenesis and biochemical assays based on the structural information and identify an XGGGX motif on keratins that can be recognized by DEC205, thereby providing insights into the interaction between DEC205 and keratins. Overall, these findings not only improve the understanding of the diverse ligand specificities of the mannose receptor family members at the molecular level but may also give clues for the interactions of keratins with their binding partners in the corresponding pathways.

Interaction of human dendritic cell receptor DEC205/CD205 with keratins.,Kong D, Qian Y, Yu B, Hu Z, Cheng C, Wang Y, Fang Z, Yu J, Xiang S, Cao L, He Y J Biol Chem. 2024 Mar;300(3):105699. doi: 10.1016/j.jbc.2024.105699. Epub 2024 , Jan 30. PMID:38301891<ref>PMID:38301891</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hbc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cao L]]
[[Category: Cheng C]]
[[Category: He Y]]
[[Category: Hu Z]]
[[Category: Kong D]]
[[Category: Yu B]]