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PDBsum entry 4gp3
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Protein binding
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PDB id
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4gp3
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PDB id:
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| Name: |
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Protein binding
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Title:
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The crystal structure of human fascin 1 k358a mutant
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Structure:
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Fascin. Chain: a, b. Synonym: 55 kda actin-bundling protein, singed-like protein, p55. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fan1, fscn1, hsn, snl. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.25Å
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R-factor:
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0.205
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R-free:
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0.252
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Authors:
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S.Y.Yang,F.K.Huang,J.Huang,S.Chen,J.Jakoncic,A.Leo-Macias,R.Diaz- Avalos,L.Chen,J.J.Zhang,X.Y.Huang
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Key ref:
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S.Yang
et al.
(2013).
Molecular mechanism of fascin function in filopodial formation.
J Biol Chem,
288,
274-284.
PubMed id:
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Date:
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20-Aug-12
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Release date:
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28-Nov-12
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PROCHECK
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Headers
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References
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Q16658
(FSCN1_HUMAN) -
Fascin from Homo sapiens
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Seq:
Struc:
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493 a.a.
480 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 1 residue position (black
cross)
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J Biol Chem
288:274-284
(2013)
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PubMed id:
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Molecular mechanism of fascin function in filopodial formation.
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S.Yang,
F.K.Huang,
J.Huang,
S.Chen,
J.Jakoncic,
A.Leo-Macias,
R.Diaz-Avalos,
L.Chen,
J.J.Zhang,
X.Y.Huang.
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ABSTRACT
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Filopodia are cell surface protrusions that are essential for cell migration.
This finger-like structure is supported by rigid tightly bundled actin
filaments. The protein responsible for actin bundling in filopodia is fascin.
However, the mechanism by which fascin functions in filopodial formation is not
clear. Here we provide biochemical, cryo-electron tomographic, and x-ray crystal
structural data demonstrating the unique structural characteristics of fascin.
Systematic mutagenesis studies on 100 mutants of fascin indicate that there are
two major actin-binding sites on fascin. Crystal structures of four fascin
mutants reveal concerted conformational changes in fascin from inactive to
active states in the process of actin bundling. Mutations in any one of the
actin-binding sites impair the cellular function of fascin in filopodial
formation. Altogether, our data reveal the molecular mechanism of fascin
function in filopodial formation.
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Links
