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PDBsum entry 5b1x

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protein ligands metals Protein-protein interface(s) links
Carbohydrate binding protein PDB id
5b1x

 

 

 

 

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Contents
Protein chains
130 a.a.
Ligands
MAN-NAG ×4
Metals
_CA ×8
Waters ×20
PDB id:
5b1x
Name: Carbohydrate binding protein
Title: Crystal structure of human dendritic cell inhibitory receptor (dcir) c-type lectin domain in complex with biantennary glycan
Structure: C-type lectin domain family 4 member a. Chain: a, b, c, d. Fragment: unp residues 106-237. Synonym: c-type lectin ddb27,c-type lectin superfamily member 6, dendritic cell immunoreceptor,lectin-like immunoreceptor. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: clec4a, clecsf6, dcir, llir, hdcgc13p. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.90Å     R-factor:   0.262     R-free:   0.290
Authors: M.Nagae,Y.Yamaguchi
Key ref: M.Nagae et al. (2016). Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan. Febs Lett, 590, 1280-1288. PubMed id: 27015765 DOI: 10.1002/1873-3468.12162
Date:
21-Dec-15     Release date:   11-May-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UMR7  (CLC4A_HUMAN) -  C-type lectin domain family 4 member A from Homo sapiens
Seq:
Struc:
237 a.a.
130 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1002/1873-3468.12162 Febs Lett 590:1280-1288 (2016)
PubMed id: 27015765  
 
 
Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan.
M.Nagae, A.Ikeda, S.Hanashima, T.Kojima, N.Matsumoto, K.Yamamoto, Y.Yamaguchi.
 
  ABSTRACT  
 
Human dendritic cell inhibitory receptor (DCIR) is a C-type lectin receptor expressed in classical dendritic cells and accepts several oligosaccharide ligands including N-glycans. Here, we report the crystal structures of human DCIR C-type lectin domains in the absence and presence of a branched N-glycan unit. The domain has a typical C-type lectin fold and two bound calcium ions. In the ligand-bound form, the disaccharide unit (GlcNAcβ1-2Man) acceptably fits the electron density map, indicating that it forms the main epitope. The recognition of the nonterminal N-glycan unit explains the relatively broad specificity of this lectin.
 

 

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