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Specific neurotrophin binding to leucine‐rich motif peptides of TrkA and TrkB
Author(s) -
Windisch Jörg M.,
Auer Bernhard,
Marksteiner Rainer,
Lang Monika E.,
Schneider Rainer
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01047-i
Subject(s) - neurotrophin , tropomyosin receptor kinase a , motif (music) , chemistry , trk receptor , leucine , leucine rich repeat , tropomyosin receptor kinase b , biochemistry , microbiology and biotechnology , biology , receptor , amino acid , neurotrophic factors , physics , acoustics
The extracellular domains of the TrkA and TrkB neurotrophin receptors contain defined structural modules such as immunoglobulin‐like domains and leucine‐rich motifs (LRMs) [Schneider and Schweiger, Oncogene 6 (1991) 1807–1811]. Recently, the second LRM of TrkA was identified as a functional nerve growth factor (NGF) binding site [Windisch et al, J. Biol. Chem. (1995) in press]. A peptide corresponding to this region effectively bound NGF and blocked binding of NGF to the recombinant extracellular domain of TrkA. The corresponding TrkB peptide exhibited the same effects with respect to brain‐derived neurotrophic factor (BDNF), neurotrophin‐3 (NT‐3), and neurotrophin‐4 (NT‐4), indicating that all three TrkB ligands utilize this same binding site. Isolated LRMs therefore embody independent functional entities.