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PDBsum entry 1oda

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protein ligands links
Lectin/immune system PDB id
1oda
Jmol
Contents
Protein chain
117 a.a. *
Ligands
BDU
* Residue conservation analysis
PDB id:
1oda
Name: Lectin/immune system
Title: N-terminal of sialoadhesin in complex with me-a-9-n- (biphenyl-4-carbonyl)-amino-9-deoxy-neu5ac (bip compound)
Structure: Sialoadhesin. Chain: a. Fragment: domain one, ig-like v-type domain, residues 20-138. Synonym: snd1, sialic acid binding ig-like lectin-1, siglec-1. Engineered: yes. Other_details: bound to me-a-9-n-(biphenyl-4-carbonyl)- amino-9-deoxy-neu5ac, coordinate system origx origx
Source: Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: cho cell. Other_details: cho cell stable expression with pee14 plasmid
Resolution:
3.31Å     R-factor:   0.217     R-free:   0.284
Authors: N.R.Zaccai,K.Maenaka,T.Maenaka,P.R.Crocker,R.Brossmer, S.Kelm,E.Y.Jones
Key ref:
N.R.Zaccai et al. (2003). Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin. Structure, 11, 557-567. PubMed id: 12737821 DOI: 10.1016/S0969-2126(03)00073-X
Date:
14-Feb-03     Release date:   14-Aug-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q62230  (SN_MOUSE) -  Sialoadhesin
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1695 a.a.
117 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/S0969-2126(03)00073-X Structure 11:557-567 (2003)
PubMed id: 12737821  
 
 
Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin.
N.R.Zaccai, K.Maenaka, T.Maenaka, P.R.Crocker, R.Brossmer, S.Kelm, E.Y.Jones.
 
  ABSTRACT  
 
The Siglec family of receptors mediates cell surface interactions through recognition of sialylated glycoconjugates. The crystal structure of the N-terminal immunoglobulin-like domain of the Siglec sialoadhesin (SnD1) in complex with 2,3-sialyllactose has informed the design of sialic acid analogs (sialosides) that bind Siglecs with significantly enhanced affinities and specificities. Binding assays against sialoadhesin (Sn; Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4) show a 10- to 300-fold reduction in IC(50) values (relative to methyl-alpha-Neu5Ac) for three sialosides bearing aromatic group modifications of the glycerol side chain: Me-alpha-9-N-benzoyl-amino-9-deoxy-Neu5Ac (BENZ), Me-alpha-9-N-(naphthyl-2-carbonyl)-amino-9-deoxy-Neu5Ac (NAP), and Me-alpha-9-N-(biphenyl-4-carbonyl)-amino-9-deoxy-Neu5Ac (BIP). Crystal structures of these sialosides in complex with SnD1 suggest explanations for the differences in specificity and affinity, providing further ideas for compound design of physiological and potentially therapeutic relevance.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Chemical Structures of Sialosides Used in This Study

 
  The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 557-567) copyright 2003.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21087105 G.J.Boons (2010).
Liposomes modified by carbohydrate ligands can target B cells for the treatment of B-cell lymphomas.
  Expert Rev Vaccines, 9, 1251-1256.  
19594633 L.Nitschke (2009).
CD22 and Siglec-G: B-cell inhibitory receptors with distinct functions.
  Immunol Rev, 230, 128-143.  
18922173 E.L.Goh, J.K.Young, K.Kuwako, M.Tessier-Lavigne, Z.He, J.W.Griffin, and G.L.Ming (2008).
beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones.
  Mol Brain, 1, 10.  
18452295 O.Blixt, S.Han, L.Liao, Y.Zeng, J.Hoffmann, S.Futakawa, and J.C.Paulson (2008).
Sialoside analogue arrays for rapid identification of high affinity siglec ligands.
  J Am Chem Soc, 130, 6680-6681.  
17722062 M.Nowicki, J.Kosacka, R.Brossmer, K.Spanel-Borowski, and J.Borlak (2007).
The myelin-associated glycoprotein inhibitor BENZ induces outgrowth and survival of rat dorsal root ganglion cell cultures.
  J Neurosci Res, 85, 3053-3063.  
17380156 P.R.Crocker, J.C.Paulson, and A.Varki (2007).
Siglecs and their roles in the immune system.
  Nat Rev Immunol, 7, 255-266.  
16732727 E.M.Rapoport, G.V.Pazynina, M.A.Sablina, P.R.Crocker, and N.V.Bovin (2006).
Probing sialic acid binding Ig-like lectins (siglecs) with sulfated oligosaccharides.
  Biochemistry (Mosc), 71, 496-504.  
15701648 A.A.Vyas, O.Blixt, J.C.Paulson, and R.L.Schnaar (2005).
Potent glycan inhibitors of myelin-associated glycoprotein enhance axon outgrowth in vitro.
  J Biol Chem, 280, 16305-16310.  
16408005 S.Han, B.E.Collins, P.Bengtson, and J.C.Paulson (2005).
Homomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking.
  Nat Chem Biol, 1, 93-97.  
15292262 Y.Ikehara, S.K.Ikehara, and J.C.Paulson (2004).
Negative regulation of T cell receptor signaling by Siglec-7 (p70/AIRM) and Siglec-9.
  J Biol Chem, 279, 43117-43125.  
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.