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PDBsum entry 2bve
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protein ligands Protein-protein interface(s) links
Immune system PDB id
2bve

 

 

 

 

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Contents
Protein chains
119 a.a. *
Ligands
PH5 ×2
Waters ×114
* Residue conservation analysis
PDB id:
2bve
Name: Immune system
Title: Structure of the n-terminal of sialoadhesin in complex with 2-phenyl- prop5ac
Structure: Sialoadhesin. Chain: a, b. Fragment: domain one, ig-like v-type domain, residues 20-138. Synonym: snd1, sialic acid binding ig-like lectin-1, siglec-1. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Cell: macrophage. Expressed in: cricetulus griseus. Expression_system_taxid: 10029.
Resolution:
2.20Å     R-factor:   0.201     R-free:   0.270
Authors: N.R.Zaccai,A.P.May,R.C.Robinson,L.D.Burtnick,P.Crocker,R.Brossmer, S.Kelm,E.Y.Jones
Key ref:
N.R.Zaccai et al. (2007). Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin. J Mol Biol, 365, 1469-1479. PubMed id: 17137591 DOI: 10.1016/j.jmb.2006.10.084
Date:
27-Jun-05     Release date:   19-Jul-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q62230  (SN_MOUSE) -  Sialoadhesin from Mus musculus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1695 a.a.
119 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2006.10.084 J Mol Biol 365:1469-1479 (2007)
PubMed id: 17137591  
 
 
Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin.
N.R.Zaccai, A.P.May, R.C.Robinson, L.D.Burtnick, 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. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1 undergoes very few structural changes on ligand binding and detail how two novel classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec dimerization. In conjunction with in silico analysis, this set of structures informs us about the design of putative ligands with enhanced binding affinities and specificities to different Siglecs, and provides data with which to test the effectiveness of different computational drug design protocols.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Compounds detailed in this study and their rIP (relative inhibitory potency against 2-Me-Neu5NAc) for sialoadhesin.
Figure 3.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 365, 1469-1479) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19598234 S.W.Fan, R.A.George, N.L.Haworth, L.L.Feng, J.Y.Liu, and M.A.Wouters (2009).
Conformational changes in redox pairs of protein structures.
  Protein Sci, 18, 1745-1765.  
19278660 Y.He, G.J.Jensen, and P.J.Bjorkman (2009).
Cryo-electron tomography of homophilic adhesion mediated by the neural cell adhesion molecule L1.
  Structure, 17, 460-471.  
18706999 M.von Itzstein (2008).
Disease-associated carbohydrate-recognising proteins and structure-based inhibitor design.
  Curr Opin Struct Biol, 18, 558-566.  
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.

 

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