spacer
spacer

PDBsum entry 1a78
Go to PDB code: 
protein ligands Protein-protein interface(s) links
Lectin PDB id
1a78

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
134 a.a. *
Ligands
YIO-GAL ×2
DTT
Waters ×46
* Residue conservation analysis
PDB id:
1a78
Name: Lectin
Title: Complex of toad ovary galectin with thio-digalactose
Structure: Galectin-1. Chain: a, b. Synonym: s-lectin galectin
Source: Bufo arenarum. Organism_taxid: 38577. Organ: ovary
Biol. unit: Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.194     R-free:   0.256
Authors: L.M.Amzel,M.A.Bianchet,H.Ahmed,G.R.Vasta
Key ref:
M.A.Bianchet et al. (2000). Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins, 40, 378-388. PubMed id: 10861929 DOI: 10.1002/1097-0134(20000815)40:3<378::AID-PROT40>3.0.CO;2-7
Date:
20-Mar-98     Release date:   14-Oct-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P56217  (LEG1_RHIAE) -  Galectin-1 from Rhinella arenarum
Seq:
Struc: 		134 a.a.
134 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1002/1097-0134(20000815)40:3<378::AID-PROT40>3.0.CO;2-7 Proteins 40:378-388 (2000)
PubMed id: 10861929  
 
 
Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes.
M.A.Bianchet, H.Ahmed, G.R.Vasta, L.M.Amzel.
 
  ABSTRACT  
 
Galectin-1, S-type beta-galactosyl-binding lectins present in vertebrate and invertebrate species, are dimeric proteins that participate in cellular adhesion, activation, growth regulation, and apoptosis. Two high-resolution crystal structures of B. arenarum galectin-1 in complex with two related carbohydrates, LacNAc and TDG, show that the topologically equivalent hydroxyl groups in the two disaccharides exhibit identical patterns of interaction with the protein. Groups that are not equivalent between the two sugars present in the second moiety of the disaccharide, interact differently with the protein, but use the same number and quality of interactions. The structures show additional protein-carbohydrate interactions not present in previously reported lectin-lactose complexes. These contacts provide an explanation for the enhanced affinity of galectin-1 for TDG and LacNAc relative to lactose. Galectins are in dimer-monomer equilibrium at physiological protein concentrations, suggesting that this equilibrium may be involved in organ-specific regulation of activity. Comparison of B. arenarum with other galectin-1 structures shows that among different galectins there are significant changes in accessible surface area buried upon dimer formation, providing a rationale for the variations observed in the free-energies of dimerization. The structure of the B. arenarum galectin-1 has a large cleft with a strong negative potential that connects the two binding sites at the surface of the protein. Such a striking characteristic suggests that this cleft is probably involved in interactions of the galectin with other intra or extra-cellular proteins. Proteins 2000;40:378-388.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Thiogalactosamine bound to B. arenarum lectin (monomer B). The relevant CRD residues and the hydrogen bonds (dashed lines) to the sugar are shown. Carbon atoms are in white, oxygen in red; sulfur in yellow; nitrogen in blue. 		Figure 5.
Figure 5. N-acetyllactosamine bound to B. arenarum lectin (monomer B). The relevant CRD residues and the hydrogen bonds (dashed lines) to the sugar are shown. The atoms are colored as in Figure 4.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2000, 40, 378-388) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21460456 E.Krissinel (2011).
Macromolecular complexes in crystals and solutions.
  Acta Crystallogr D Biol Crystallogr, 67, 376-385.  
19421996 E.Krissinel (2010).
Crystal contacts as nature's docking solutions.
  J Comput Chem, 31, 133-143.  
19938027 E.Wéber, A.Hetényi, B.Váczi, E.Szolnoki, R.Fajka-Boja, V.Tubak, E.Monostori, and T.A.Martinek (2010).
Galectin-1-asialofetuin interaction is inhibited by peptides containing the tyr-xxx-tyr motif acting on the glycoprotein.
  Chembiochem, 11, 228-234.  
19444247 G.R.Vasta (2009).
Roles of galectins in infection.
  Nat Rev Microbiol, 7, 424-438.  
19437454 S.J.Chen, N.T.Chen, S.H.Wang, J.C.Hsu, W.H.Ding, L.L.Kuo-Huang, and R.N.Huang (2009).
Insecticidal action of mammalian galectin-1 against diamondback moth (Plutella xylostella).
  Pest Manag Sci, 65, 923-930.  
18275083 B.C.Lee, K.Park, and D.Kim (2008).
Analysis of the residue-residue coevolution network and the functionally important residues in proteins.
  Proteins, 72, 863-872.  
18320588 D.Zhou, H.Ge, J.Sun, Y.Gao, M.Teng, and L.Niu (2008).
Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins.
  Proteins, 71, 1582-1588.
PDB code: 3b9c
16990264 M.Nagae, N.Nishi, T.Murata, T.Usui, T.Nakamura, S.Wakatsuki, and R.Kato (2006).
Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition.
  J Biol Chem, 281, 35884-35893.
PDB codes: 2d6k 2d6l 2d6m 2d6n 2d6o 2d6p
16972013 T.Shirai, C.Shionyu-Mitsuyama, T.Ogawa, and K.Muramoto (2006).
Structure based studies of the adaptive diversification process of congerins.
  Mol Divers, 10, 567-573.  
15465324 G.R.Vasta, H.Ahmed, and E.W.Odom (2004).
Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates.
  Curr Opin Struct Biol, 14, 617-630.  
15543683 S.Kamhawi, M.Ramalho-Ortigao, V.M.Pham, S.Kumar, P.G.Lawyer, S.J.Turco, C.Barillas-Mury, D.L.Sacks, and J.G.Valenzuela (2004).
A role for insect galectins in parasite survival.
  Cell, 119, 329-341.  
12829506 L.He, S.André, H.C.Siebert, H.Helmholz, B.Niemeyer, and H.J.Gabius (2003).
Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and x-ray scattering.
  Biophys J, 85, 511-524.  
14517974 M.G.Ford, T.Weimar, T.Köhli, and R.J.Woods (2003).
Molecular dynamics simulations of galectin-1-oligosaccharide complexes reveal the molecular basis for ligand diversity.
  Proteins, 53, 229-240.  
12646584 N.Maeda, N.Kawada, S.Seki, T.Arakawa, K.Ikeda, H.Iwao, H.Okuyama, J.Hirabayashi, K.Kasai, and K.Yoshizato (2003).
Stimulation of proliferation of rat hepatic stellate cells by galectin-1 and galectin-3 through different intracellular signaling pathways.
  J Biol Chem, 278, 18938-18944.  
11585829 M.Bilej, P.De Baetselier, E.Van Dijck, B.Stijlemans, A.Colige, and A.Beschin (2001).
Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize Gram-negative and Gram-positive bacteria.
  J Biol Chem, 276, 45840-45847.  
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.

 

spacer
spacer