8hbc

Crystal structure of the CysR-CTLD3 fragment of human DEC205

spinqualitylabelsall models 8hbc, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hbc is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.35Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA