PDBsum entry 3kqg

Immune system

PDB id

3kqg

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Contents

			Protein chains

					169 a.a. *


					157 a.a. *

			Metals

					_CA ×6

			Waters ×407

* Residue conservation analysis

PDB id:

3kqg

Links

Name:

Immune system

Title:

Trimeric structure of langerin

Structure:

C-type lectin domain family 4 member k. Chain: a, b, c, d, e, f. Fragment: unp residues 147-328. Synonym: langerin. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cd207, clec4k. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å

R-factor:

0.185

R-free:

0.239

Authors:

H.Feinberg,A.S.Powlesland,M.E.Taylor,W.I.Weis

Key ref:

H.Feinberg et al. (2010). Trimeric structure of langerin. J Biol Chem, 285, 13285-13293. PubMed id: 20181944

Date:

17-Nov-09

Release date:

23-Feb-10

PROCHECK

	Headers

	References

Protein chain

Q9UJ71 (CLC4K_HUMAN) - C-type lectin domain family 4 member K from Homo sapiens

Seq: Struc:					328 a.a. 169 a.a.*

Protein chains

Q9UJ71 (CLC4K_HUMAN) - C-type lectin domain family 4 member K from Homo sapiens

Seq: Struc:					328 a.a. 157 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

	J Biol Chem 285:13285-13293 (2010)
PubMed id: 20181944

Trimeric structure of langerin.
H.Feinberg, A.S.Powlesland, M.E.Taylor, W.I.Weis.

ABSTRACT

Langerin, an endocytic receptor of Langerhans cells, binds pathogens such as human immunodeficiency virus by recognition of surface glycoconjugates and mediates their internalization into Birbeck granules. Langerin has an extracellular region consisting of a C-type carbohydrate-recognition domain (CRD) and a neck region that stabilizes formation of trimers. As in many other C-type lectins, oligomerization is required for high affinity binding to glycan ligands and is also likely to be important for determining specificity. To facilitate structural analysis of the human langerin trimer, a truncated form of the extracellular region, consisting of part of the neck and the CRD, has been characterized. Like the full-length protein, truncated langerin exists as a stable trimer in solution. Glycan array screening with the trimeric fragment shows that high mannose oligosaccharides are the best ligands for langerin. Structural analysis of the trimeric fragment of langerin confirms that the neck region forms a coiled-coil of alpha-helices. Multiple interactions between the neck region and the CRDs make the trimer a rigid unit with the three CRDs in fixed positions and the primary sugar-binding sites separated by a distance of 42 A. The fixed orientation of the sugar-binding sites in the trimer is likely to place constraints on the ligands that can be bound by langerin.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21112338

H.Feinberg, M.E.Taylor, N.Razi, R.McBride, Y.A.Knirel, S.A.Graham, K.Drickamer, and W.I.Weis (2011).
Structural basis for langerin recognition of diverse pathogen and mammalian glycans through a single binding site.

J Mol Biol, 405, 1027-1039.

PDB codes:

3p5d 3p5e 3p5f 3p5g 3p5h 3p5i

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.