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PDBsum entry 1jzn
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Sugar binding protein
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PDB id
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1jzn
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Crystal structure of a galactose-specific c-type lectin
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Structure:
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Galactose-specific lectin. Chain: a, b, c, d, e. Synonym: rsl (rattlesnake lectin)
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Source:
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Crotalus atrox. Western diamondback rattlesnake. Organism_taxid: 8730. Other_details: isolated from venom
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Biol. unit:
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Pentamer (from PDB file)
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Resolution:
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2.20Å
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R-factor:
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0.198
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R-free:
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0.251
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Authors:
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J.R.Walker,B.Nagar,N.M.Young,T.Hirama,J.M.Rini
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Key ref:
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J.R.Walker
et al.
(2004).
X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure.
Biochemistry,
43,
3783-3792.
PubMed id:
DOI:
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Date:
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16-Sep-01
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Release date:
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01-Jul-03
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PROCHECK
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Headers
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References
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P21963
(LECG_CROAT) -
C-type lectin Cal from Crotalus atrox
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Seq:
Struc:
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135 a.a.
135 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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DOI no:
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Biochemistry
43:3783-3792
(2004)
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PubMed id:
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X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure.
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J.R.Walker,
B.Nagar,
N.M.Young,
T.Hirama,
J.M.Rini.
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ABSTRACT
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Rattlesnake venom lectin (RSL) from the western diamondback rattlesnake
(Crotalus atrox) is an oligomeric galactose-specific C-type lectin. The X-ray
crystal structure of RSL, in complex with lactose and thiodigalactoside, at 2.2
and 2.3 A resolution, respectively, reveals a decameric protein composed of two
5-fold symmetric pentamers arranged in a staggered, back-to-back orientation.
Each monomer corresponds to a single canonical C-type lectin carbohydrate
recognition domain devoid of accessory domains and is disulfide-bonded to a
monomer in the other pentamer. The structure is the first example of that of a
carbohydrate complex of a vertebrate galactose-specific C-type lectin. The 10
carbohydrate-binding sites, located on the rim of the decamer, suggest a role
for multivalent interactions and a mechanism for RSL's ability to promote
receptor cross-linking and cell aggregation.
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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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D.R.Rokyta,
K.P.Wray,
A.R.Lemmon,
E.M.Lemmon,
and
S.B.Caudle
(2011).
A high-throughput venom-gland transcriptome for the Eastern Diamondback Rattlesnake (Crotalus adamanteus) and evidence for pervasive positive selection across toxin classes.
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Toxicon,
57,
657-671.
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E.d.o.s. .S.Nunes,
M.A.de Souza,
A.F.Vaz,
G.M.Santana,
F.S.Gomes,
L.C.Coelho,
P.M.Paiva,
R.M.da Silva,
R.A.Silva-Lucca,
M.L.Oliva,
M.C.Guarnieri,
and
M.T.Correia
(2011).
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom.
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Comp Biochem Physiol B Biochem Mol Biol,
159,
57-63.
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R.Doley,
and
R.M.Kini
(2009).
Protein complexes in snake venom.
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Cell Mol Life Sci,
66,
2851-2871.
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A.D.Hill,
and
P.J.Reilly
(2008).
A Gibbs free energy correlation for automated docking of carbohydrates.
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J Comput Chem,
29,
1131-1141.
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H.Feinberg,
M.E.Taylor,
and
W.I.Weis
(2007).
Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism.
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J Biol Chem,
282,
17250-17258.
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PDB codes:
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A.N.Zelensky,
and
J.E.Gready
(2005).
The C-type lectin-like domain superfamily.
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FEBS J,
272,
6179-6217.
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J.M.Mancheño,
H.Tateno,
I.J.Goldstein,
M.Martínez-Ripoll,
and
J.A.Hermoso
(2005).
Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
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J Biol Chem,
280,
17251-17259.
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PDB codes:
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R.L.Rich,
and
D.G.Myszka
(2005).
Survey of the year 2004 commercial optical biosensor literature.
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J Mol Recognit,
18,
431-478.
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G.Xu,
M.Teng,
L.Niu,
P.Liu,
Y.Dong,
Q.Liu,
Q.Huang,
and
Q.Hao
(2004).
Purification, characterization, crystallization and preliminary X-ray crystallographic analysis of two novel C-type lectin-like proteins: Aall-A and Aall-B from Deinagkistrodon acutus venom.
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Acta Crystallogr D Biol Crystallogr,
60,
2035-2037.
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H.Sugawara,
M.Kusunoki,
G.Kurisu,
T.Fujimoto,
H.Aoyagi,
and
T.Hatakeyama
(2004).
Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis.
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J Biol Chem,
279,
45219-45225.
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PDB codes:
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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
codes are
shown on the right.
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Links
