8JAH

Crystal structure of human CLEC12A C-type lectin domain

Summary for 8JAH

• Entry DOI: 10.2210/pdb8jah/pdb
• Descriptor: C-type lectin domain family 12 member A, SULFATE ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: receptor, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 29226.24

Authors

Lei, Q.,Tang, H.,Dong, X. (deposition date: 2023-05-06, release date: 2024-03-13, Last modification date: 2024-04-03)

Primary citation

Tang, H.,Xiao, Y.,Qian, L.,Wang, Z.,Lu, M.,Yao, N.,Zhou, T.,Tian, F.,Cao, L.,Zheng, P.,Dong, X.
Mechanistic insights into the C-type lectin receptor CLEC12A-mediated immune recognition of monosodium urate crystal.
J.Biol.Chem., 300:105765-105765, 2024

PubMed Abstract: CLEC12A, a member of the C-type lectin receptor family involved in immune homeostasis, recognizes MSU crystals released from dying cells. However, the molecular mechanism underlying the CLEC12A-mediated recognition of MSU crystals remains unclear. Herein, we reported the crystal structure of the human CLEC12A-C-type lectin-like domain (CTLD) and identified a unique "basic patch" site on CLEC12A-CTLD that is necessary for the binding of MSU crystals. Meanwhile, we determined the interaction strength between CLEC12A-CTLD and MSU crystals using single-molecule force spectroscopy. Furthermore, we found that CLEC12A clusters at the cell membrane and seems to serve as an internalizing receptor of MSU crystals. Altogether, these findings provide mechanistic insights for understanding the molecular mechanisms underlying the interplay between CLEC12A and MSU crystals.

PubMed: 38367667
DOI: 10.1016/j.jbc.2024.105765

Experimental method

X-RAY DIFFRACTION (2.58 Å)