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PDBsum entry 1fwv

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Sugar binding protein PDB id
1fwv
Jmol
Contents
Protein chain
134 a.a. *
Ligands
SGA-MAG-FUC
Waters ×127
* Residue conservation analysis
PDB id:
1fwv
Name: Sugar binding protein
Title: Crystal structure of the cysteine-rich domain of mannose receptor complexed with 3-so4-lewis(a)
Structure: Cysteine-rich domain of mannose receptor. Chain: a. Fragment: n-terminal domain of mannose receptor. Engineered: yes. Other_details: complexed with 3-so4-lewis(a)
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: sus scrofa. Expression_system_taxid: 9823. Expression_system_cell: 293 cells
Resolution:
2.20Å     R-factor:   0.208     R-free:   0.230
Authors: Y.Liu,Z.Misulovin,P.J.Bjorkman
Key ref:
Y.Liu et al. (2001). The molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor. J Mol Biol, 305, 481-490. PubMed id: 11152606 DOI: 10.1006/jmbi.2000.4326
Date:
24-Sep-00     Release date:   17-Jan-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q61830  (MRC1_MOUSE) -  Macrophage mannose receptor 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1456 a.a.
134 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1006/jmbi.2000.4326 J Mol Biol 305:481-490 (2001)
PubMed id: 11152606  
 
 
The molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor.
Y.Liu, Z.Misulovin, P.J.Bjorkman.
 
  ABSTRACT  
 
The mannose receptor (MR) binds foreign and host ligands through interactions with their carbohydrates. Two portions of MR have distinct carbohydrate recognition properties. One is conferred by the amino-terminal cysteine-rich domain (Cys-MR), which plays a critical role in binding sulfated glycoproteins including pituitary hormones. The other is achieved by tandemly arranged C-type lectin domains that facilitate carbohydrate-dependent uptake of infectious microorganisms. This dual carbohydrate binding specificity enables MR to bind ligands by interacting with both sulfated and non-sulfated polysaccharide chains. We previously determined crystal structures of Cys-MR complexed with 4-SO(4)-N-acetylglucosamine and with an unidentified ligand resembling Hepes (N-[2-hydroxyethyl]piperazine-N'-[2-ethanesulfonic acid]). In continued efforts to elucidate the mechanism of sulfated carbohydrate recognition by Cys-MR, we characterized the binding affinities between Cys-MR and potential carbohydrate ligands using a fluorescence-based assay. We find that Cys-MR binds sulfated carbohydrates with relatively high affinities (K(D)=0.1 mM to 1.0 mM) compared to the affinities of other lectins. Cys-MR also binds Hepes with a K(D) value of 3.9 mM, consistent with the suggestion that the ligand in the original Cys-MR crystal structure is Hepes. We also determined crystal structures of Cys-MR complexed with 3-SO(4)-Lewis(x), 3-SO(4)-Lewis(a), and 6-SO(4)-N-acetylglucosamine at 1.9 A, 2.2 A, and 2.5 A resolution, respectively, and the 2.0 A structure of Cys-MR that had been treated to remove Hepes. The conformation of the Cys-MR binding site is virtually identical in all Cys-MR crystal structures, suggesting that Cys-MR does not undergo conformational changes upon ligand binding. The structures are used to rationalize the binding affinities derived from the biochemical studies and to elucidate the molecular mechanism of sulfated carbohydrate recognition by Cys-MR.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure of Cys-MR bound to 4-SO[4]-GalNAc. Ribbon diagram of the Cys-MR structure with lobes I, II, and III indicated in different colors. Disulfide bonds are yellow and 4-SO[4]-GalNAc is shown in ball-and-stick representation. Trp117 is highlighted in blue.
Figure 5.
Figure 5. Comparson of Cys-MR binding to 3-SO[4]-Gal and 4-SO[4]-GalNAc. Stereo view of the interactions between Cys-MR and the 3-SO[4]-Gal portion of 3-SO[4]-Lewisx and 4-SO[4]-GalNAc. Hydrogen bonds between ligand and protein atoms are indicated by dotted green lines.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 305, 481-490) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
15234974 L.Tao, and A.L.Harris (2004).
Biochemical requirements for inhibition of Connexin26-containing channels by natural and synthetic taurine analogs.
  J Biol Chem, 279, 38544-38554.  
15162495 R.Koike, K.Kinoshita, and A.Kidera (2004).
Probabilistic description of protein alignments for sequences and structures.
  Proteins, 56, 157-166.  
12730367 N.Armstrong, M.Mayer, and E.Gouaux (2003).
Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.
  Proc Natl Acad Sci U S A, 100, 5736-5741.
PDB codes: 1p1n 1p1o 1p1q 1p1u 1p1w
11785767 H.Kogelberg, and T.Feizi (2001).
New structural insights into lectin-type proteins of the immune system.
  Curr Opin Struct Biol, 11, 635-643.  
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.