WeightNameValue
1000 Titel
  • Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity
1000 Autor/in
  1. Ball, Linda J. |
  2. Kühne, Ronald |
  3. Hoffmann, Berit |
  4. Häfner, Angelika |
  5. Volkmer‐Engert, Rudolf |
  6. Hof, Martin |
  7. Wahl, Martin |
  8. Schneider‐Mergener, Jens |
  9. Walter, Ulrich |
  10. Oschkinat, Hartmut |
  11. Jarchau, Thomas |
  12. Schmieder, Peter |
1000 Erscheinungsjahr 2000
1000 LeibnizOpen
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2000-09-15
1000 Erschienen in
1000 Quellenangabe
  • 19(18): 4903-4914
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC314220/ |
  • https://dx.doi.org/10.1093/emboj/19.18.4903 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • The Ena‐VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N‐terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize ‘FPPPP’ motifs found in the mammalian zyx in and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1–peptide interactions are strongly dependent on the recognition of residues flanking the core FPPPP motifs. Determination of the VASP EVH1 domain solution structure, together with peptide library screening, measurement of individual Kds by fluorescence titration, and NMR chemical shift mapping, revealed a second affinity‐determining epitope present in all four ActA EVH1‐binding motifs. The epitope was shown to interact with a complementary hydrophobic site on the EVH1 surface and to increase strongly the affinity of ActA for EVH1 domains. We propose that this epitope, which is absent in the sequences of the native EVH1‐interaction partners zyxin and vinculin, may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell.
1000 Sacherschließung
lokal ActA
lokal FPPPP motif
lokal protein complex
lokal EVH1 domain
lokal zyxin
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/QmFsbCwgTGluZGEgSi4=|https://frl.publisso.de/adhoc/creator/S8O8aG5lLCBSb25hbGQ=|https://frl.publisso.de/adhoc/creator/SG9mZm1hbm4sIEJlcml0|https://frl.publisso.de/adhoc/creator/SMOkZm5lciwgQW5nZWxpa2E=|https://frl.publisso.de/adhoc/creator/Vm9sa21lcuKAkEVuZ2VydCwgUnVkb2xm|https://frl.publisso.de/adhoc/creator/SG9mLCBNYXJ0aW4=|https://frl.publisso.de/adhoc/creator/V2FobCwgTWFydGlu|https://frl.publisso.de/adhoc/creator/U2NobmVpZGVy4oCQTWVyZ2VuZXIsIEplbnM=|https://frl.publisso.de/adhoc/creator/V2FsdGVyLCBVbHJpY2g=|https://frl.publisso.de/adhoc/creator/T3NjaGtpbmF0LCBIYXJ0bXV0|https://frl.publisso.de/adhoc/creator/SmFyY2hhdSwgVGhvbWFz|http://orcid.org/0000-0001-9968-9327
1000 Förderer
  1. EMBO |
  2. Deutsche Forschungsgemeinschaft |
  3. Czech Academy of Sciences |
1000 Fördernummer
  1. -
  2. -
  3. -
1000 Förderprogramm
  1. -
  2. -
  3. -
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer EMBO |
    1000 Förderprogramm -
    1000 Fördernummer -
  2. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft |
    1000 Förderprogramm -
    1000 Fördernummer -
  3. 1000 joinedFunding-child
    1000 Förderer Czech Academy of Sciences |
    1000 Förderprogramm -
    1000 Fördernummer -
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6404470.rdf
1000 Erstellt am 2017-09-15T13:53:50.904+0200
1000 Erstellt von 122
1000 beschreibt frl:6404470
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Wed Aug 01 12:41:33 CEST 2018
1000 Objekt bearb. Wed Aug 01 12:41:32 CEST 2018
1000 Vgl. frl:6404470
1000 Oai Id
  1. oai:frl.publisso.de:frl:6404470 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
1000 Gegenstand von

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