8K8H
Crystal structure of the CysR-CTLD3 fragment of human DEC205
8K8H の概要
エントリーDOI | 10.2210/pdb8k8h/pdb |
分子名称 | Lymphocyte antigen 75 (2 entities in total) |
機能のキーワード | dec 205, cd205, keratin, dead cell, immune system, recombination |
由来する生物種 | Homo sapiens |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 68312.42 |
構造登録者 | |
主引用文献 | Kong, D.,Qian, Y.,Yu, B.,Hu, Z.,Cheng, C.,Wang, Y.,Fang, Z.,Yu, J.,Xiang, S.,Cao, L.,He, Y. Interaction of human dendritic cell receptor DEC205/CD205 with keratins. J.Biol.Chem., 300:105699-105699, 2024 Cited by PubMed Abstract: 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∼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. PubMed: 38301891DOI: 10.1016/j.jbc.2024.105699 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.79 Å) |
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