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PDBsum entry 6v1c
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Sugar binding protein
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PDB id
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6v1c
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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 human trefoil factor 3 in complex with its cognate ligand
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Structure:
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Trefoil factor 3. Chain: a. Synonym: intestinal trefoil factor,hitf,polypeptide p1.B,hp1.B. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: tff3, itf, tfi. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.55Å
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R-factor:
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0.175
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R-free:
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0.188
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Authors:
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M.A.Jarva,J.P.Lingford,A.John,N.E.Scott,E.D.Goddard-Borger
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Key ref:
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M.A.Järvå
et al.
(2020).
Trefoil factors share a lectin activity that defines their role in mucus.
Nat Commun,
11,
2265.
PubMed id:
DOI:
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Date:
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20-Nov-19
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Release date:
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11-Dec-19
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PROCHECK
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Headers
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References
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Q07654
(TFF3_HUMAN) -
Trefoil factor 3 from Homo sapiens
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Seq:
Struc:
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80 a.a.
53 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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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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Nat Commun
11:2265
(2020)
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PubMed id:
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Trefoil factors share a lectin activity that defines their role in mucus.
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M.A.Järvå,
J.P.Lingford,
A.John,
N.M.Soler,
N.E.Scott,
E.D.Goddard-Borger.
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ABSTRACT
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The mucosal epithelium secretes a host of protective disulfide-rich peptides,
including the trefoil factors (TFFs). The TFFs increase the viscoelasticity of
the mucosa and promote cell migration, though the molecular mechanisms
underlying these functions have remained poorly defined. Here, we demonstrate
that all TFFs are divalent lectins that recognise the GlcNAc-α-1,4-Gal
disaccharide, which terminates some mucin-like O-glycans. Degradation of this
disaccharide by a glycoside hydrolase abrogates TFF binding to mucins.
Structural, mutagenic and biophysical data provide insights into how the TFFs
recognise this disaccharide and rationalise their ability to modulate the
physical properties of mucus across different pH ranges. These data reveal that
TFF activity is dependent on the glycosylation state of mucosal glycoproteins
and alludes to a lectin function for trefoil domains in other human proteins.
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Links
