Biomaterial Database

Three dimensional structure of the soybean agglutinin Gal/GalNAc complexes by homology modeling. 1998

V S Rao, and K Lam, and P K Qasba

Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, National Cancer Institute, NCI-FCRDC, Frederick, Maryland 21702, USA.

Complexes of soybean agglutinin (SBA) with galactose (Gal) and N-acetyl galactosamine (GalNAc) have been modeled based on its homology to erythrina corallodendron (EcorL) lectin. The three dimensional structure of SBA-Gal modeled with homology techniques agrees well with SBA-(beta-LacNAc)2Gal-R complex determined by X-ray crystallographic techniques at the beta-sheet regions and the regions where Ca2+ and Mn2+ ions bind. However, significant deviations have been observed between the modeled and the X-ray structures, particularly at the loop regions where the polypeptide chain could not be unequivocally traced in the X-ray structure. The hydrogen bonding scheme, predicted from the homology model, shows that the invariant residues i.e. Asp, Gly, Asn, and aromatic residues (Phe) found in all other legume lectins, bind Gal, slightly in a different way than reported in X-ray structure of SBA-pentasaccharide complex. The higher binding affinity of GalNAc over Gal to SBA is due to additional hydrophobic interactions with Tyr107 rather than a hydrogen bond between N-acetamide group of the sugar and the side chain of Asp88 as suggested from X-ray crystal structure studies. Our modeling also suggest that the variation in the length of the loop D observed among galactose binding legume lectins may not have any effect on the binding of sugar at the monosaccharide specific site of the lectins. Soybean agglutinin (SBA) is a member of the leguminous family of lectins. They generally possess a single carbohydrate binding site, besides the tightly bound Ca2+ and Mn2+ ions which are required for their carbohydrate binding activity. They possess a high degree of sequence homology and about 50% of the amino acid residues are invariant. Some of these invariant amino acid residues are involved in the binding of sugar moieties and in metal ion coordination. X-ray crystallographic studies showed that their three-dimensional structures are very similar, though they differ in their carbohydrate binding specificity (1-6). Three of the invariant residues Asp, Gly, and Asn, besides an aromatic residue (Phe or Tyr), are involved in carbohydrate binding. Independent of their sugar specificity, these four residues in legume lectins provide the basic frame for the sugar to bind.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D003198	Computer Simulation	Computer-based representation of physical systems and phenomena such as chemical processes.	Computational Modeling,Computational Modelling,Computer Models,In silico Modeling,In silico Models,In silico Simulation,Models, Computer,Computerized Models,Computer Model,Computer Simulations,Computerized Model,In silico Model,Model, Computer,Model, Computerized,Model, In silico,Modeling, Computational,Modeling, In silico,Modelling, Computational,Simulation, Computer,Simulation, In silico,Simulations, Computer
D005690	Galactose	An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.	D-Galactose,Galactopyranose,Galactopyranoside,D Galactose
D000116	Acetylgalactosamine	The N-acetyl derivative of galactosamine.	2-Acetamido-2-D-galactopyranose,2-Acetamido-2-Deoxy-D-Galactose,2-Acetamido-2-Deoxygalactose,N-Acetyl-D-Galactosamine,2 Acetamido 2 D galactopyranose,2 Acetamido 2 Deoxy D Galactose,2 Acetamido 2 Deoxygalactose,N Acetyl D Galactosamine
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D017386	Sequence Homology, Amino Acid	The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.	Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D030262	Soybean Proteins	Proteins which are present in or isolated from SOYBEANS.	Dietary Soybean Protein,Soy Bean Protein,Soybean Protein,Dietary Soybean Proteins,Soy Bean Proteins,Soy Protein,Soy Proteins,Bean Protein, Soy,Protein, Dietary Soybean,Protein, Soy,Protein, Soy Bean,Protein, Soybean,Proteins, Dietary Soybean,Proteins, Soy,Soybean Protein, Dietary,Soybean Proteins, Dietary