 |
PDBsum entry 3wbq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Carbohydrate binding protein
|
PDB id
|
|
|
|
3wbq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (bdca2) reveal a common domain-Swapped dimer.
|
|
|
Authors
|
|
M.Nagae,
A.Ikeda,
Y.Kitago,
N.Matsumoto,
K.Yamamoto,
Y.Yamaguchi.
|
|
|
Ref.
|
|
Proteins, 2014,
82,
1512-1518.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
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. Proteins 2014; 82:1512-1518. © 2013 Wiley
Periodicals, Inc.
|
|
|
|
|
|
|
