3WBP

Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-1)

Summary for 3WBP

• Entry DOI: 10.2210/pdb3wbp/pdb
• Related: 3WBQ 3WBR
• Descriptor: C-type lectin domain family 4 member C, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: c-type lectin fold, immune receptor, complex-type n-glycan, carbohydrate binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single-pass type II membrane protein : Q8WTT0
• Total number of polymer chains: 2
• Total formula weight: 36302.59

Authors

Nagae, M.,Ikeda, A.,Kitago, Y.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y. (deposition date: 2013-05-20, release date: 2013-12-25, Last modification date: 2024-10-30)

Primary citation

Nagae, M.,Ikeda, A.,Kitago, Y.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y.
Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer.
Proteins, 82:1512-1518, 2014

PubMed Abstract: We report on crystal structures of a carbohydrate recognition domain (CRD) of human C-type lectin receptor blood dendritic cell antigen-2 (BDCA2). Three different crystal forms were obtained at 1.8-2.3 Å resolution. In all three, the CRD has a basic C-type lectin fold, but a long loop extends away from the core domain to form a domain-swapped dimer. The structures of the dimers from the three different crystal forms superimpose well, indicating that domain swapping and dimer formation are energetically stable. The structure of the dimer is compared with other domain-swapped proteins, and a possible regulation mechanism of BDCA2 is discussed.

PubMed: 24425442
DOI: 10.1002/prot.24504

Experimental method

X-RAY DIFFRACTION (1.8 Å)