PDBsum entry 2ox9

Sugar binding protein

PDB id

2ox9

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Contents

			Protein chains

					130 a.a. *

			Ligands

					NAG-FUC-GAL ×4

			Metals

					_CA ×16

			Waters ×357

* Residue conservation analysis

PDB id:

2ox9

Links

Name:

Sugar binding protein

Title:

Mouse scavenger receptor c-type lectin carbohydrate-recognition domain.

Structure:

Collectin placenta 1. Chain: a, b, c, d. Fragment: crd domain. Synonym: collectin sub-family member 12. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: colec12, cl-p1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.95Å

R-factor:

0.224

R-free:

0.273

Authors:

W.I.Weis,H.Feinberg,K.Drickamer,M.E.Taylor

Key ref:

H.Feinberg et al. (2007). Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism. J Biol Chem, 282, 17250-17258. PubMed id: 17420244 DOI: 10.1074/jbc.M701624200

Date:

20-Feb-07

Release date:

03-Apr-07

PROCHECK

	Headers

	References

Protein chains

Q8K4Q8 (COL12_MOUSE) - Collectin-12 from Mus musculus

Seq: Struc:

Seq: Struc:					742 a.a. 130 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1074/jbc.M701624200	J Biol Chem 282:17250-17258 (2007)
PubMed id: 17420244

Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism.
H.Feinberg, M.E.Taylor, W.I.Weis.

ABSTRACT

The scavenger receptor C-type lectin (SRCL) is unique in the family of class A scavenger receptors, because in addition to binding sites for oxidized lipoproteins it also contains a C-type carbohydrate-recognition domain (CRD) that interacts with specific glycans. Both human and mouse SRCL are highly specific for the Lewisx trisaccharide, which is commonly found on the surfaces of leukocytes and some tumor cells. Structural analysis of the CRD of mouse SRCL in complex with Lewisx and mutagenesis show the basis for this specificity. The interaction between mouse SRCL and Lewisx is analogous to the way that selectins and DC-SIGN bind to related fucosylated glycans, but the mechanism of the interaction is novel, because it is based on a primary galactose-binding site similar to the binding site in the asialoglycoprotein receptor. Crystals of the human receptor lacking bound calcium ions reveal an alternative conformation in which a glycan ligand would be released during receptor-mediated endocytosis.

Selected figure(s)



	Figure 2. FIGURE 2. Structure of the CRD from SRCL. The CRD is shown as a color ramp starting with blue at the N terminus and ending in red at the C terminus. Disulfide bonds are shown in yellow. A, human SRCL. Zn^2+ are shown as orange spheres. B, mouse SRCL bound to Lewis^x. The oligosaccharide is shown in a stick representation. Ca^2+ are shown as large green spheres.		Figure 5. FIGURE 5. Comparison of galactose-binding sites in C-type CRDs. Carbon, nitrogen, oxygen, and calcium are represented as white, blue, red, and green spheres, respectively. Hydrogen bonds are shown as dashed gray lines, Ca^2+ coordination bonds are dashed black lines and hydrophobic interactions are in dashed blue lines. A, mouse SRCL. For simplicity only the galactose residue of Lewis^x is shown. B, Gal/GalNAc-binding mutant of mannose-binding protein complexed with GalNAc (1FIH, copy A) (16). C, rattlesnake venom lectin complexed with lactose (1JZN) (17). D, tunicate lectin complexed with galactose (1TLG) (18).

Figures were selected by an automated process.

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

19433864

A.S.Powlesland, P.G.Hitchen, S.Parry, S.A.Graham, M.M.Barrio, M.T.Elola, J.Mordoh, A.Dell, K.Drickamer, and M.E.Taylor (2009).
Targeted glycoproteomic identification of cancer cell glycosylation.

Glycobiology, 19, 899-909.

19528664

M.E.Taylor, and K.Drickamer (2009).
Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands.

Glycobiology, 19, 1155-1162.

19805264

W.Wang, T.Hu, P.A.Frantom, T.Zheng, B.Gerwe, D.S.Del Amo, S.Garret, R.D.Seidel, and P.Wu (2009).
Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives.

Proc Natl Acad Sci U S A, 106, 16096-16101.

19424029

X.Wang, X.Yang, S.Cui, Y.Yan, and Z.Yang (2009).
A novel pseudovirus containing lewis X oligosaccharides with pD-L1 targeting to DCs induces T cells tolerance.

Transplantation, 87, 1305-1307.

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

18790731

M.Sakakura, S.Oo-Puthinan, C.Moriyama, T.Kimura, J.Moriya, T.Irimura, and I.Shimada (2008).
Carbohydrate binding mechanism of the macrophage galactose-type C-type lectin 1 revealed by saturation transfer experiments.

J Biol Chem, 283, 33665-33673.

17942297

M.E.Taylor, and K.Drickamer (2007).
Paradigms for glycan-binding receptors in cell adhesion.

Curr Opin Cell Biol, 19, 572-577.

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 code is shown on the right.