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PDBsum entry 4d4u
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Sugar binding protein
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PDB id
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4d4u
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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 fucose binding lectin from aspergillus fumigatus (afl) in complex with lewisy tetrasaccharide.
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Structure:
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Fucose-specific lectin flea. Chain: a, b. Synonym: afl. Engineered: yes
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Source:
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Aspergillus fumigatus. Organism_taxid: 746128. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.99Å
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R-factor:
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0.172
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R-free:
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0.220
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Authors:
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J.Houser,J.Komarek,N.Kostlanova,M.Lahmann,G.Cioci,A.Varrot,A.Imberty, M.Wimmerova
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Key ref:
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J.Houser
et al.
(2015).
Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.
Acta Crystallogr D Biol Crystallogr,
71,
442-453.
PubMed id:
DOI:
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Date:
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31-Oct-14
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Release date:
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11-Mar-15
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Supersedes:
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PROCHECK
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Headers
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References
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Q4WW81
(LECF_ASPFU) -
Fucose-specific lectin from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
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Seq:
Struc:
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315 a.a.
314 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 3 residue positions (black
crosses)
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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:442-453
(2015)
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PubMed id:
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Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.
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J.Houser,
J.Komarek,
G.Cioci,
A.Varrot,
A.Imberty,
M.Wimmerova.
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ABSTRACT
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The Aspergillus fumigatus lectin AFL was recently described as a new member of
the AAL lectin family. As a lectin from an opportunistic pathogen, it might play
an important role in the interaction of the pathogen with the human host. A
detailed study of structures of AFL complexed with several monosaccharides and
oligosaccharides, including blood-group epitopes, was combined with affinity
data from SPR and discussed in the context of previous findings. Its six binding
sites are non-equivalent, and owing to minor differences in amino-acid
composition they exhibit a marked difference in specific ligand recognition. AFL
displays a high affinity in the micromolar range towards oligosaccharides which
were detected in plants and also those bound on the human epithelia. All of
these results indicate AFL to be a complex member of the lectin family and a
challenging target for future medical research and, owing to its binding
properties, a potentially useful tool in specific biotechnological applications.
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Links
