1B8M

BRAIN DERIVED NEUROTROPHIC FACTOR, NEUROTROPHIN-4

1B8M の概要

• エントリーDOI: 10.2210/pdb1b8m/pdb
• 分子名称: PROTEIN (BRAIN DERIVED NEUROTROPHIC FACTOR), PROTEIN (NEUROTROPHIN-4) (3 entities in total)
• 機能のキーワード: complex (growth factor-growth factor), neurotrophin, growth factor-neurotrophin-4 complex, growth factor/neurotrophin-4
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27480.22

構造登録者

Robinson, R.C.,Radziejewski, C.,Stuart, D.I.,Jones, E.Y.,Choe, S. (登録日: 1999-02-01, 公開日: 1999-02-09, 最終更新日: 2024-11-20)

主引用文献

Robinson, R.C.,Radziejewski, C.,Spraggon, G.,Greenwald, J.,Kostura, M.R.,Burtnick, L.D.,Stuart, D.I.,Choe, S.,Jones, E.Y.
The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site.
Protein Sci., 8:2589-2597, 1999

PubMed Abstract: The neurotrophins are growth factors that are involved in the development and survival of neurons. Neurotrophin release by a target tissue results in neuron growth along the neurotrophin concentration gradient, culminating in the eventual innervation of the target tissue. These activities are mediated through trk cell surface receptors. We have determined the structures of the heterodimer formed between brain-derived neurotrophic factor (BDNF) and neurotrophin 4 (NT4), as well as the structure of homodimer of NT4. We also present the structure of the Neurotrophin 3 homodimer, which is refined to higher resolution than previously published. These structures provide the first views of the architecture of the NT4 protomer. Comparison of the surface of a model of the BDNF homodimer with the structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors. In particular, there exists an analogous region on the surface of each neurotrophin that is likely to be involved in trk receptor binding. Variations in sequence on the periphery of this common region serve to confer trk receptor specificity.

PubMed: 10631974

実験手法

X-RAY DIFFRACTION (2.75 Å)