Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BRAIN-DERIVED NEUROTROPHIC FACTOR, NEUROTROPHIN-3, AND NEUROTROPHIN-4BIND TO A SINGLE LEUCINE-RICH MOTIF OF TRKB
Autore:
WINDISCH JM; MARKSTEINER R; LANG ME; AUER B; SCHNEIDER R;
Indirizzi:
INNSBRUCK UNIV,INST BIOCHEM,PETER MAYR STR 1A A-6020 INNSBRUCK AUSTRIA INNSBRUCK UNIV,INST BIOCHEM A-6020 INNSBRUCK AUSTRIA
Titolo Testata:
Biochemistry
fascicolo: 35, volume: 34, anno: 1995,
pagine: 11256 - 11263
SICI:
0006-2960(1995)34:35<11256:BNFNAN>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
NERVE GROWTH-FACTOR; TYROSINE PROTEIN-KINASE; AFFINITY NGF RECEPTOR; PROTOONCOGENE PRODUCT; GLYCOSYLATION; ADHESION; NEURONS; DOMAIN; DEATH; SIMILARITIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
78
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Windisch et al., "BRAIN-DERIVED NEUROTROPHIC FACTOR, NEUROTROPHIN-3, AND NEUROTROPHIN-4BIND TO A SINGLE LEUCINE-RICH MOTIF OF TRKB", Biochemistry, 34(35), 1995, pp. 11256-11263

Abstract

TrkB is a member of the Trk family of neurotrophin receptors. Its extracellular domain exhibits the same modular structure found in its homologs, TrkA and TrkC, consisting of an N-terminal LRM(3) cassette and two immunoglobulin-like modules (Ig2 domain) adjacent to the membrane. The LRM(3) cassette comprises two cysteine-rich clusters framing a tandem array of three leucine-rich motifs (LRMs). On the basis of the recent identification of a nerve growth factor (HGF) binding site withinTrMA, the ability of the different structural entities within the extracellular domain of TrkB to bind the various neurotrophins was determined by using a recombinant receptor approach. Brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4) bound to the LRM(3) cassette of TrkB, whereas NGF did not. These bindingcharacteristics evidently reflect in vivo specificities. A more precise mapping of the region(s) responsible for binding BDNF, NT-3, and NT-4 identified the second leucine-rich motif of TrkB as a functional unit capable of binding all three neurotrophins. The affinities and kinetics that this short stretch of amino acids exhibited with respect to the different neurotrophins were clearly akin to those observed for cells ectopically expressing TrkB receptors. With 24 amino acids determining the affinities and kinetics of the interactions with three different partners, the leucine-rich motif is strongly established as one ofthe most potent and flexible protein-protein interaction motifs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/06/20 alle ore 22:20:36