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PDBsum entry 3bbs

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protein metals Protein-protein interface(s) links
Immune system PDB id
3bbs
Jmol
Contents
Protein chains
129 a.a. *
Metals
_CA ×4
Waters ×286
* Residue conservation analysis
Superseded by: 3p7f
PDB id:
3bbs
Name: Immune system
Title: The carbohydrate recognition domain of langerin reveals high structural similarity with the one of dc-sign but an additi calcium-independent sugar-binding site
Structure: C-type lectin domain family 4 member k. Chain: a, b, c, d. Fragment: residues unp 197-325. Synonym: langerin, cd207 antigen, apo-structure langerin. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: langerin. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.200     R-free:   0.240
Authors: L.Chatwell,A.Holla,B.Kaufer,A.Skerra
Key ref: L.Chatwell et al. (2008). The carbohydrate recognition domain of Langerin reveals high structural similarity with the one of DC-SIGN but an additional, calcium-independent sugar-binding site. Mol Immunol, 45, 1981-1994. PubMed id: 18061677 DOI: 10.1016/j.molimm.2007.10.030
Date:
11-Nov-07     Release date:   25-Dec-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UJ71  (CLC4K_HUMAN) -  C-type lectin domain family 4 member K
Seq:
Struc:
328 a.a.
129 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.molimm.2007.10.030 Mol Immunol 45:1981-1994 (2008)
PubMed id: 18061677  
 
 
The carbohydrate recognition domain of Langerin reveals high structural similarity with the one of DC-SIGN but an additional, calcium-independent sugar-binding site.
L.Chatwell, A.Holla, B.B.Kaufer, A.Skerra.
 
  ABSTRACT  
 
Langerin is a type II transmembrane oligosaccharide receptor on Langerhans cells (LCs), a prominent subclass of dendritic cells (DCs) that mediate immune responses in epithelia and play a role in HIV degradation. Its extracellular moiety comprises a neck region with several heptad repeats and an exposed carboxy-terminal calcium-type carbohydrate-recognition domain (CRD). The CRD of human Langerin, which was expressed as a soluble protein in the periplasm of E. coli, was crystallized both alone and in the presence of two sugars, followed by X-ray analyses to resolutions of 2.5A for apo-Langerin and to 1.6A and 2.1A for the complexes with mannose and maltose, respectively. The fold of the Langerin CRD (dubbed LangA) resembles that of other typical C-type lectins such as DC-SIGN. However, especially in the long loop region (LLR), which is responsible for carbohydrate-binding, two additional secondary structure elements are present: a 3(10) helix and a small beta-sheet arising from the extended beta-strand 2, which enters into a hairpin and a new strand beta2'. Unexpectedly, the crystal structures in the presence of maltose and mannose reveal two sugar-binding sites. One is calcium-dependent and structurally conserved in the C-type lectin family whereas the second one represents a novel, calcium-independent type. Based on these data, a model for the binding of mannan, a component of many endogenous as well as viral glycoproteins, is proposed and the differences in binding behavior between Langerin and DC-SIGN with respect to the Lewis X carbohydrate antigen and its derivatives can be explained. Therefore, the crystal structure of LangA should be helpful for the development of new marker reagents selective for LCs and also of therapeutic compounds that may enhance the inhibitory role of Langerin towards HIV infection.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20181944 H.Feinberg, A.S.Powlesland, M.E.Taylor, and W.I.Weis (2010).
Trimeric structure of langerin.
  J Biol Chem, 285, 13285-13293.
PDB code: 3kqg
20026605 H.Tateno, K.Ohnishi, R.Yabe, N.Hayatsu, T.Sato, M.Takeya, H.Narimatsu, and J.Hirabayashi (2010).
Dual specificity of Langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain.
  J Biol Chem, 285, 6390-6400.  
21030306 M.A.de Jong, and T.B.Geijtenbeek (2010).
Langerhans cells in innate defense against pathogens.
  Trends Immunol, 31, 452-459.  
20309013 M.van der Vlist, and T.B.Geijtenbeek (2010).
Langerin functions as an antiviral receptor on Langerhans cells.
  Immunol Cell Biol, 88, 410-415.  
20382864 R.E.Lehotzky, C.L.Partch, S.Mukherjee, H.L.Cash, W.E.Goldman, K.H.Gardner, and L.V.Hooper (2010).
Molecular basis for peptidoglycan recognition by a bactericidal lectin.
  Proc Natl Acad Sci U S A, 107, 7722-7727.  
19224860 J.Lai, O.K.Bernhard, S.G.Turville, A.N.Harman, J.Wilkinson, and A.L.Cunningham (2009).
Oligomerization of the Macrophage Mannose Receptor Enhances gp120-mediated Binding of HIV-1.
  J Biol Chem, 284, 11027-11038.  
19756298 R.D.Cummings (2009).
The repertoire of glycan determinants in the human glycome.
  Mol Biosyst, 5, 1087-1104.  
19287024 S.T.Hollmig, K.Ariizumi, and P.D.Cruz (2009).
Recognition of non-self-polysaccharides by C-type lectin receptors dectin-1 and dectin-2.
  Glycobiology, 19, 568-575.  
19171971 T.Lütteke (2009).
Analysis and validation of carbohydrate three-dimensional structures.
  Acta Crystallogr D Biol Crystallogr, 65, 156-168.  
18687680 J.P.Gourdine, G.Cioci, L.Miguet, C.Unverzagt, D.V.Silva, A.Varrot, C.Gautier, E.J.Smith-Ravin, and A.Imberty (2008).
High affinity interaction between a bivalve C-type lectin and a biantennary complex-type N-glycan revealed by crystallography and microcalorimetry.
  J Biol Chem, 283, 30112-30120.
PDB codes: 2vuv 2vuz
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