Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins. (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1074/jbc.M401184200 (literal)

Alternative label

• Gazzarrini S.; Kang M.; Van Etten J.L.; Tayefeh S.; Kast S.M.; DiFrancesco D.; Thiel G.; Moroni A. (2004)
  Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins.
  in The Journal of biological chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Gazzarrini S.; Kang M.; Van Etten J.L.; Tayefeh S.; Kast S.M.; DiFrancesco D.; Thiel G.; Moroni A. (literal)

Pagina inizio

• 28443 (literal)

Pagina fine

• 28449 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 279 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 27 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Gazzarrini S.:Department of Biology Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; Kang M., Van Etten J.L.: Department of Plant Pathology and Nebraska Center for Virology, University of Nebraska, Lincoln, Nebraska 68583-0722; Tayefeh S., Kast S.M.: Institute for Inorganic and Physical Chemistry and §§Botany, Darmstadt University of Technology, 64287 Darmstadt, Germany; DiFrancesco D.: Department of Biomolecular Sciences and Biotechnology, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; Thiel G.: Institute for Botany, Darmstadt University of Technology, 64287 Darmstadt, Germany; Moroni A.: Department of Biology Università degli Studi di Milano and Consiglio Nazionale delle Ricerche Istituto di Biofisica-Mi, Via Celoria 26, 20133 Milano, Italy; (literal)

Titolo

• Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins. (literal)

Abstract

• Kcv is a 94-amino acid protein encoded by chlorella virus PBCV-1 that corresponds to the pore module of K(+) channels. Therefore, Kcv can be a model for studying the protein design of K(+) channel pores. We analyzed the molecular diversity generated by approximately 1 billion years of evolution on kcv genes isolated from 40 additional chlorella viruses. Because the channel is apparently required for virus replication, the Kcv variants are all functional and contain multiple and dispersed substitutions that represent a repertoire of allowed sets of amino acid substitutions (from 4 to 12 amino acids). Correlations between amino acid substitutions and the new properties displayed by these channels guided site-directed mutations that revealed synergistic amino acid interactions within the protein as well as previously unknown interactions between distant channel domains. The effects of these multiple changes were not predictable from a priori structural knowledge of the channel pore. (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)

Autore CNR

• ANNA MORONI (Persona)

Insieme di parole chiave

• Keywords of "Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins." (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)

Autore CNR di

• ANNA MORONI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?Journal of biological chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins." (Insieme di parole chiave)