Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin

Journal of Molecular Biology

Volumn 302, Issue 5, 2000, Pages 1129-1137

  Manoj, N ^a   Srinivas, V R ^a   Surolia, A ^a   Vijayan, M ^a   Suguna, K ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Carbohydrate binding; H antigenic specificity; Legume lectin; Protein crystallography; Protein carbohydrate interactions

Indexed keywords

AGGLUTININ; BLOOD GROUP O ANTIGEN; CARBOHYDRATE; EPITOPE; GALACTOSE; LECTIN; PROTEIN SUBUNIT;

ANTIGEN SPECIFICITY; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIMERIZATION; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; THERMODYNAMICS;

ERYTHRINA CORALLODENDRON; PHASEOLUS (ANGIOSPERM); PSOPHOCARPUS TETRAGONOLOBUS;

EID: 0034613013     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4111     Document Type: Article

References (59)

1. Thermodynamic analysis of ligand binding to winged bean (Psophocarpus tetragonolobus) acidic agglutinin reveals its specificity for terminally monofucosylated H-reactive sugars
2. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
3. Coformation, protein-carbohydrate interactions and a novel subunit association in the refined strucure of peanut lectin-lactose complex
4. OMITMAP: An electron density map suitable for examination of errors in a macromolecular model
5. Novel structures of plant lectins and their complexes with carbohydrates
6. The crystal structures of Man(α1-3)Man(α1-O)Me and Man(α1-6)Man(α1-O)Me in complex with concanavalin A
7. X-ray and molecular dynamics studies of concanavalin-A glucoside and mannoside complexes. Relating structure to thermodynamics of binding
8. Crystallography and NMR System (CNS): A new software system for macromolecular structure determination
9. Calorimetric analysis of the binding of lectins with overlapping carbohydrate-binding ligand specificities
10. A database analysis of potential glycosylating Asn-X-Ser/Thr consensus sequences
11. Analytical molecular surface calculation
12. Making a fitting choice: Common aspects of sugar-binding sites in plant and animal lectins
13. Structures of the Erythrina corallodendron lectin and of its complexes with mono and disaccharides
14. Accurate bond and angle parameters for X-ray protein structure refinement
15. Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus
16. Structure of concanavalin A at 2.4 Å resolution
17. Computer simulation of histoblood group oligosaccharides: Energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens
18. Improved methods for building protein models in electron density maps and the location of errors in these models
19. Thermodynamic and kinetic analysis of carbohydrate binding to the basic lectin from winged bean (Psophocarpus tetragonolobus)
20. Halloween ... masks and bones
21. Phi/psi-chology: Ramachandran revisited
22. Characterization of the acidic lectins from winged bean seed (Psophocarpus tetragonolobus)
23. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
24. PROCHECK: A program to check the stereochemical quality of protein structures
25. Shape complementarity at protein-protein interfaces
26. Lectins: Carbohydrate-specific proteins that mediate cellular recognition
27. Review: Legume lectin structure
28. Traitement statistique des erreurs dans la determination des structures cristallines
29. Crystallisation and preliminary crystallographic analysis of winged bean acidic lectin
30. Structure of basic winged bean lectin and a comparison with its saccharide bound form
31. Concanavalin A distorts the β-GlcNAc-(1,2)-Man linkage of β-GlcNAc-(1,2)-α-Man-(1,3)-[β-GlcNAc-(1,2)-α-Man-(1,6)]-Man upon binding
32. Man α1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
33. Redefinition of the carbohydrate specificity of Erythrina corallodendron lectin based on solid-phase binding assays and molecular modelling of native and recombinant forms obtained by site-directed mutagenesis
34. AMoRe: An automated package for molecular replacement
35. Erythrocyte-binding studies on an acidic lectin from winged bean (Psophocarpus tetragonolobus)
36. A statistical analysis of N- and O-glycan linkage conformations from crystallographic data
37. Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å resolution
38. Variability in quaternary association of proteins with the same tertiary fold: A case-study and rationalization involving legume lectins
39. Stereochemistry of polypeptide chain configuration
40. Structures of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins
41. Lectin structure
42. The detection of sub-units within the crystallographic asymmetric unit
43. Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates
44. Lectins as cell recognition molecules
45. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
46. Analysis of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity
47. The thermodynamics of the carbohydrate binding to the H-antigen specific lectin from Psophocarpus tetragonolobus
48. A predominantly hydrophobic recognition of H-antigenic sugars by winged bean acidic lectin: A thermodynamic study
49. Thermodynamics of monosaccharide binding to Erythrina corallodendron lectin
50. Structure and energetics of protein carbohydrate complexes
51. Phase evaluation and some aspects of the Fourier refinement of macromolecules
52. Lectins
53. Structural basis of lectin-carbohydrate recognition
54. Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding sites
55. An evaluation of the use of databases in protein structure refinement