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PDBsum entry 1vln
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* Residue conservation analysis
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PDB id:
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Lectin
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Title:
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A triclinic crystal form of the lectin concanavalin a
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Structure:
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Concanavalin a. Chain: a, b, c, d, e, f, g, h
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Source:
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Canavalia ensiformis. Jack bean. Organism_taxid: 3823
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Biol. unit:
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Tetramer (from
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Resolution:
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2.40Å
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R-factor:
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0.205
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R-free:
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0.265
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Authors:
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P.N.Kanellopoulos,P.A.Tucker,S.J.Hamodrakas
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Key ref:
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P.N.Kanellopoulos
et al.
(1996).
A Triclinic Crystal Form of the Lectin Concanavalin A
J Struct Biol,
117,
16-23.
PubMed id:
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Date:
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03-Apr-96
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Release date:
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01-Apr-97
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PROCHECK
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Headers
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References
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P08902
(LECA_DIOGR) -
Lectin alpha chain from Dioclea grandiflora
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Seq: Struc:
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237 a.a.
237 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 43 residue positions (black
crosses)
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J Struct Biol
117:16-23
(1996)
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PubMed id:
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A Triclinic Crystal Form of the Lectin Concanavalin A
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P.N.Kanellopoulos,
P.A.Tucker,
K.Pavlou,
B.Agianian,
S.J.Hamodrakas.
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ABSTRACT
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The molecular structure of a triclinic crystal form of concanavalin A has been
refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A,
b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma =
97.5degrees and contain two tetramers per asymmetric unit each with approximate
222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor
is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer
is more similar to that found in concanavalin A saccharide complexes than in the
previously reported I222 crystal form of uncomplexed concanavalin A. A
comparison of the molecular packing between the two crystal forms shows a more
open arrangement with large solvent channels through the crystal.
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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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W.Vornholt,
M.Hartmann,
and
M.Keusgen
(2007).
SPR studies of carbohydrate-lectin interactions as useful tool for screening on lectin sources.
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Biosens Bioelectron,
22,
2983-2988.
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F.B.Moreno,
G.A.Bezerra,
T.M.de Oliveira,
E.P.de Souza,
B.A.da Rocha,
R.G.Benevides,
P.Delatorre,
B.S.Cavada,
and
W.F.de Azevedo
(2006).
New crystal forms of Diocleinae lectins in the presence of different dimannosides.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
1100-1103.
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M.Hartmann,
P.Nikitin,
and
M.Keusgen
(2006).
Innovative analytical system for screening on lectins.
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Biosens Bioelectron,
22,
28-34.
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F.J.López-Jaramillo,
L.A.González-Ramírez,
A.Albert,
F.Santoyo-González,
A.Vargas-Berenguel,
and
F.Otálora
(2004).
Structure of concanavalin A at pH 8: bound solvent and crystal contacts.
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Acta Crystallogr D Biol Crystallogr,
60,
1048-1056.
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PDB code:
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T.V.Ratto,
K.C.Langry,
R.E.Rudd,
R.L.Balhorn,
M.J.Allen,
and
M.W.McElfresh
(2004).
Force spectroscopy of the double-tethered concanavalin-A mannose bond.
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Biophys J,
86,
2430-2437.
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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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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.
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