TI  - Interactions between  <prot>brain-derived neurotrophic factor</prot>  and the  <prot><prot>TRKB</prot>
      receptor</prot> . Identification of two ligand binding domains in soluble <prot>TRKB</prot> by
      affinity separation and chemical cross-linking.
PG  - 25296-303
AB  - The extracellular domain of the human <prot>neurotrophin  <prot>TRKB</prot> receptor</prot>  expressed
      in Chinese hamster ovary cells is a highly glycosylated protein,
      possessing binding ability for  <prot>brain-derived neurotrophic factor</prot> (<prot>BDNF</prot>) .
      Two distinct ligand binding domains of <prot>TRKB</prot> were isolated from proteolytic
      digests of the receptor by affinity separation on immobilized <prot>BDNF</prot>. One of
      these domains consists of amino acid residues 103-181 and contains both
      the third leucine-rich motif and the second cysteine cluster domain. The
      second domain is close to the second immunoglobulin-like domain (amino
      acid residues 342-394). Each of these two domains can bind <prot>BDNF</prot>
      independently. Disulfide linkages present in the first domain are
      necessary for <prot>BDNF</prot> binding, probably because of preservation of the native
      conformation. To study the second domain in greater detail, a truncated
      form of <prot>TRKB</prot> containing the second immunoglobulin-like domain (residues
      248-398) was expressed in Escherichia coli. This domain was cross-linked
      to <prot>BDNF</prot> through a 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide coupling
      reaction. Several synthetic peptides corresponding to amino acid residues
      343-379 were able to bind immobilized <prot>BDNF</prot>. Amino acid substitution and
      cross-linking analysis indicated that amino acids Phe347, Asp354, and
      Tyr361 are intimately involved in <prot>BDNF</prot> binding. These results, obtained
      from a variety of experimental techniques, highlight the importance of two
      distinct regions of the extracellular domain of the  <prot><prot>TRKB</prot> receptor</prot>  in
      binding  <prot>BDNF</prot> .
AD  - Departments of Protein Structure, Protein Chemistry, and Immunology,
