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PDBsum entry 3cna
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Lectin (agglutinin)
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PDB id
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3cna
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
11:4910-4919
(1972)
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PubMed id:
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Structure of concanavalin A at 2.4-A resolution.
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K.D.Hardman,
C.F.Ainsworth.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.A.Rocha,
P.Delatorre,
T.M.Oliveira,
R.G.Benevides,
A.F.Pires,
A.A.Sousa,
L.A.Souza,
A.M.Assreuy,
H.Debray,
W.F.de Azevedo,
A.H.Sampaio,
and
B.S.Cavada
(2011).
Structural basis for both pro- and anti-inflammatory response induced by mannose-specific legume lectin from Cymbosema roseum.
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Biochimie,
93,
806-816.
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PDB code:
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M.Ali,
P.Ramirez,
M.N.Tahir,
S.Mafe,
Z.Siwy,
R.Neumann,
W.Tremel,
and
W.Ensinger
(2011).
Biomolecular conjugation inside synthetic polymer nanopores via glycoprotein-lectin interactions.
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Nanoscale,
3,
1894-1903.
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Y.Iiguni,
and
H.Watarai
(2010).
Dynamic electromagnetophoretic force analysis of a single binding interaction between lectin and mannan polysaccharide on yeast cell surface.
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Analyst,
135,
1426-1432.
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M.Dhayal,
and
D.M.Ratner
(2009).
XPS and SPR analysis of glycoarray surface density.
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Langmuir,
25,
2181-2187.
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Y.P.Kim,
S.Park,
E.Oh,
Y.H.Oh,
and
H.S.Kim
(2009).
On-chip detection of protein glycosylation based on energy transfer between nanoparticles.
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Biosens Bioelectron,
24,
1189-1194.
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F.Naseem,
and
R.H.Khan
(2008).
Structural intermediates of acid unfolded Con-A in different co-solvents: fluoroalcohols and polyethylene glycols.
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Int J Biol Macromol,
42,
158-165.
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K.A.Kulkarni,
S.Katiyar,
A.Surolia,
M.Vijayan,
and
K.Suguna
(2008).
Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectin.
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Acta Crystallogr D Biol Crystallogr,
64,
730-737.
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PDB codes:
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N.Sharon
(2007).
Lectins: carbohydrate-specific reagents and biological recognition molecules.
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J Biol Chem,
282,
2753-2764.
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L.Buts,
A.Garcia-Pino,
A.Imberty,
N.Amiot,
G.J.Boons,
S.Beeckmans,
W.Versées,
L.Wyns,
and
R.Loris
(2006).
Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin.
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FEBS J,
273,
2407-2420.
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PDB codes:
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R.Ballerstadt,
C.Evans,
R.McNichols,
and
A.Gowda
(2006).
Concanavalin A for in vivo glucose sensing: a biotoxicity review.
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Biosens Bioelectron,
22,
275-284.
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S.Sinha,
N.Mitra,
G.Kumar,
K.Bajaj,
and
A.Surolia
(2005).
Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account.
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Biophys J,
88,
1300-1310.
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F.B.Moreno,
P.Delatorre,
B.T.Freitas,
B.A.Rocha,
E.P.Souza,
F.Facó,
F.Canduri,
A.L.Cardoso,
V.N.Freire,
J.L.Lima Filho,
A.H.Sampaio,
J.J.Calvete,
W.F.De Azevedo,
and
B.S.Cavada
(2004).
Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia gladiata seeds.
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Acta Crystallogr D Biol Crystallogr,
60,
1493-1495.
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N.Mitra,
N.Sharon,
and
A.Surolia
(2003).
Role of N-linked glycan in the unfolding pathway of Erythrina corallodendron lectin.
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Biochemistry,
42,
12208-12216.
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N.Mitra,
V.R.Srinivas,
T.N.Ramya,
N.Ahmad,
G.B.Reddy,
and
A.Surolia
(2002).
Conformational stability of legume lectins reflect their different modes of quaternary association: solvent denaturation studies on concanavalin A and winged bean acidic agglutinin.
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Biochemistry,
41,
9256-9263.
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S.Parkin,
and
G.Craig
(2002).
Crystallization and X-ray diffraction data for a new form of concanavalin A.
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Acta Crystallogr D Biol Crystallogr,
58,
1032-1033.
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D.Jain,
K.J.Kaur,
and
D.M.Salunke
(2001).
Plasticity in protein-peptide recognition: crystal structures of two different peptides bound to concanavalin A.
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Biophys J,
80,
2912-2921.
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PDB codes:
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I.Grishkovskaya,
G.V.Avvakumov,
G.Sklenar,
D.Dales,
G.L.Hammond,
and
Y.A.Muller
(2000).
Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain.
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EMBO J,
19,
504-512.
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PDB code:
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G.B.Reddy,
V.R.Srinivas,
N.Ahmad,
and
A.Surolia
(1999).
Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization.
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J Biol Chem,
274,
4500-4503.
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M.M.Prabu,
K.Suguna,
and
M.Vijayan
(1999).
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins.
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Proteins,
35,
58-69.
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M.Vijayan,
and
N.Chandra
(1999).
Lectins.
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Curr Opin Struct Biol,
9,
707-714.
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N.Manoj,
V.R.Srinivas,
and
K.Suguna
(1999).
Structure of basic winged-bean lectin and a comparison with its saccharide-bound form.
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Acta Crystallogr D Biol Crystallogr,
55,
794-800.
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PDB code:
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R.Ravishankar,
K.Suguna,
A.Surolia,
and
M.Vijayan
(1999).
Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins.
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Acta Crystallogr D Biol Crystallogr,
55,
1375-1382.
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PDB codes:
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S.D.Wood,
L.M.Wright,
C.D.Reynolds,
P.J.Rizkallah,
A.K.Allen,
W.J.Peumans,
and
E.J.Van Damme
(1999).
Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 A resolution.
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Acta Crystallogr D Biol Crystallogr,
55,
1264-1272.
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PDB code:
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D.A.Rozwarski,
B.M.Swami,
C.F.Brewer,
and
J.C.Sacchettini
(1998).
Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates.
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J Biol Chem,
273,
32818-32825.
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PDB code:
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L.Mourey,
J.D.Pédelacq,
C.Birck,
C.Fabre,
P.Rougé,
and
J.P.Samama
(1998).
Crystal structure of the arcelin-1 dimer from Phaseolus vulgaris at 1.9-A resolution.
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J Biol Chem,
273,
12914-12922.
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PDB code:
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T.K.Dam,
B.S.Cavada,
T.B.Grangeiro,
C.F.Santos,
F.A.de Sousa,
S.Oscarson,
and
C.F.Brewer
(1998).
Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates.
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J Biol Chem,
273,
12082-12088.
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T.K.Dam,
S.Oscarson,
J.C.Sacchettini,
and
C.F.Brewer
(1998).
Differential solvation of "core" trimannoside complexes of the Dioclea grandiflora lectin and concanavalin A detected by primary solvent isotope effects in isothermal titration microcalorimetry.
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J Biol Chem,
273,
32826-32832.
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V.Chu,
S.Freitag,
I.Le Trong,
R.E.Stenkamp,
and
P.S.Stayton
(1998).
Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system.
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Protein Sci,
7,
848-859.
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PDB codes:
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W.Cheng,
E.Bullitt,
L.Bhattacharyya,
C.F.Brewer,
and
L.Makowski
(1998).
Electron microscopy and x-ray diffraction studies of Lotus tetragonolobus A isolectin cross-linked with a divalent Lewisx oligosaccharide, an oncofetal antigen.
|
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J Biol Chem,
273,
35016-35022.
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C.Chothia,
T.Hubbard,
S.Brenner,
H.Barns,
and
A.Murzin
(1997).
Protein folds in the all-beta and all-alpha classes.
|
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Annu Rev Biophys Biomol Struct,
26,
597-627.
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G.Sulzenbacher,
M.Schülein,
and
G.J.Davies
(1997).
Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
|
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Biochemistry,
36,
5902-5911.
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PDB codes:
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T.B.Grangeiro,
A.Schriefer,
J.J.Calvete,
M.Raida,
C.Urbanke,
M.Barral-Netto,
and
B.S.Cavada
(1997).
Molecular cloning and characterization of ConBr, the lectin of Canavalia brasiliensis seeds.
|
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Eur J Biochem,
248,
43-48.
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S.Jain,
W.B.Drendel,
Z.W.Chen,
F.S.Mathews,
W.S.Sly,
and
J.H.Grubb
(1996).
Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs.
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Nat Struct Biol,
3,
375-381.
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PDB code:
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J.Antosiewicz
(1995).
Computation of the dipole moments of proteins.
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Biophys J,
69,
1344-1354.
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J.Bouckaert,
R.Loris,
F.Poortmans,
and
L.Wyns
(1995).
Crystallographic structure of metal-free concanavalin A at 2.5 A resolution.
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Proteins,
23,
510-524.
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PDB code:
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F.Jurnak,
M.D.Yoder,
R.Pickersgill,
and
J.Jenkins
(1994).
Parallel beta-domains: a new fold in protein structures.
|
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Curr Opin Struct Biol,
4,
802-806.
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N.Srinivasan,
H.E.White,
J.Emsley,
S.P.Wood,
M.B.Pepys,
and
T.L.Blundell
(1994).
Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.
|
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Structure,
2,
1017-1027.
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PDB codes:
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R.Banerjee,
S.C.Mande,
V.Ganesh,
K.Das,
V.Dhanaraj,
S.K.Mahanta,
K.Suguna,
A.Surolia,
and
M.Vijayan
(1994).
Crystal structure of peanut lectin, a protein with an unusual quaternary structure.
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Proc Natl Acad Sci U S A,
91,
227-231.
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PDB code:
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S.D.Rufino,
and
T.L.Blundell
(1994).
Structure-based identification and clustering of protein families and superfamilies.
|
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J Comput Aided Mol Des,
8,
5.
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M.D.Yoder,
S.E.Lietzke,
and
F.Jurnak
(1993).
Unusual structural features in the parallel beta-helix in pectate lyases.
|
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Structure,
1,
241-251.
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PDB code:
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D.Bassolino-Klimas,
and
R.E.Bruccoleri
(1992).
Application of a directed conformational search for generating 3-D coordinates for protein structures from alpha-carbon coordinates.
|
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Proteins,
14,
465-474.
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A.Rivera-Sagredo,
D.Solis,
T.Diaz-Mauriño,
J.Jiménez-Barbero,
and
M.Martín-Lomas
(1991).
Studies on the molecular recognition of synthetic methyl beta-lactoside analogs by ricin, a cytotoxic plant lectin.
|
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Eur J Biochem,
197,
217-228.
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D.L.Meadows,
and
J.S.Schultz
(1991).
A molecular model for singlet/singlet energy transfer of monovalent ligand/receptor interactions.
|
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Biotechnol Bioeng,
37,
1066-1075.
|
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A.Bernad,
J.M.Lázaro,
M.Salas,
and
L.Blanco
(1990).
The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization.
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Proc Natl Acad Sci U S A,
87,
4610-4614.
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M.M.Yamashita,
L.Wesson,
G.Eisenman,
and
D.Eisenberg
(1990).
Where metal ions bind in proteins.
|
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Proc Natl Acad Sci U S A,
87,
5648-5652.
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G.Barone,
G.Castronuovo,
P.Del Vecchio,
V.Elia,
and
P.Guarrata
(1989).
Binding of lanthanum and gadolinium ions to concanavalin A studied calorimetrically at 25 degrees C.
|
| |
J Mol Recognit,
2,
147-151.
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Z.Derewenda,
J.Yariv,
J.R.Helliwell,
A.J.Kalb,
E.J.Dodson,
M.Z.Papiz,
T.Wan,
and
J.Campbell
(1989).
The structure of the saccharide-binding site of concanavalin A.
|
| |
EMBO J,
8,
2189-2193.
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PDB code:
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P.Argos
(1988).
A sequence motif in many polymerases.
|
| |
Nucleic Acids Res,
16,
9909-9916.
|
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M.C.Manning,
and
R.W.Woody
(1987).
Theoretical determination of the CD of proteins containing closely packed antiparallel beta-sheets.
|
| |
Biopolymers,
26,
1731-1752.
|
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M.Lüscher-Mattli
(1987).
The thermodynamic parameters of the interaction of concanavalin A with glycosyl-free liposomes: a microcalorimetric study.
|
| |
Biopolymers,
26,
1509-1526.
|
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W.G.Hol,
L.M.Halie,
and
C.Sander
(1981).
Dipoles of the alpha-helix and beta-sheet: their role in protein folding.
|
| |
Nature,
294,
532-536.
|
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P.Argos,
T.Tsukihara,
and
M.G.Rossmann
(1980).
A structural comparison of concanavalin A and tomato bushy stunt virus protein.
|
| |
J Mol Evol,
15,
169-179.
|
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B.A.Cunningham,
J.J.Hemperly,
T.P.Hopp,
and
G.M.Edelman
(1979).
Favin versus concanavalin A: Circularly permuted amino acid sequences.
|
| |
Proc Natl Acad Sci U S A,
76,
3218-3222.
|
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G.Stubbs,
S.Warren,
and
E.Mandelkow
(1979).
Structural comparisons of the aggregates of tobacco mosaic virus protein.
|
| |
J Supramol Struct,
12,
177-183.
|
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G.N.Reeke,
J.W.Becker,
and
G.M.Edelman
(1978).
Changes in the three-dimensional structure of concanavalin A upon demetallization.
|
| |
Proc Natl Acad Sci U S A,
75,
2286-2290.
|
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G.E.Schulz
(1977).
Structural rules for globular proteins.
|
| |
Angew Chem Int Ed Engl,
16,
23-32.
|
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A.R.Fraser,
J.J.Hemperly,
J.L.Wang,
and
G.M.Edelman
(1976).
Monovalent derivatives of concanavalin A.
|
| |
Proc Natl Acad Sci U S A,
73,
790-794.
|
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B.J.Fuhr,
B.H.Barber,
and
J.P.Carver
(1976).
Magnetic resonance studies of concanavalin A: location of the binding site of alpha-methyl-D-mannopyranoside.
|
| |
Proc Natl Acad Sci U S A,
73,
322-326.
|
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G.D.Fasman,
P.Y.Chou,
and
A.J.Adler
(1976).
Prediction of the conformation of the histones.
|
| |
Biophys J,
16,
1201-1238.
|
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J.W.Becker,
G.N.Reeke,
B.A.Cunningham,
and
G.M.Edelman
(1976).
New evidence on the location of the saccharide-binding site of concanavalin A.
|
| |
Nature,
259,
406-409.
|
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M.Levitt,
and
C.Chothia
(1976).
Structural patterns in globular proteins.
|
| |
Nature,
261,
552-558.
|
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F.Friedberg
(1974).
Effects of metal binding on protein structure.
|
| |
Q Rev Biophys,
7,
1.
|
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J.P.Privat,
F.Delmotte,
G.Mialonier,
P.Bouchard,
and
M.Monsigny
(1974).
Fluorescence studies of saccharide binding to wheat-germ agglutinin (lectin).
|
| |
Eur J Biochem,
47,
5.
|
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C.I.Brändén,
H.Eklund,
B.Nordström,
T.Boiwe,
G.Söderlund,
E.Zeppezauer,
I.Ohlsson,
and
A.Akeson
(1973).
Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution.
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| |
Proc Natl Acad Sci U S A,
70,
2439-2442.
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|
|
|
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E.A.Kabat,
and
T.T.Wu
(1973).
The influence of nearest-neighbor amino acids on the conformation of the middle amino acid in proteins: comparison of predicted and experimental determination of -sheets in concanavalin A.
|
| |
Proc Natl Acad Sci U S A,
70,
1473-1477.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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.
|
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Links
