1CNT

CILIARY NEUROTROPHIC FACTOR

1CNT の概要

• エントリーDOI: 10.2210/pdb1cnt/pdb
• 分子名称: CILIARY NEUROTROPHIC FACTOR, SULFATE ION, YTTERBIUM (III) ION, ... (4 entities in total)
• 機能のキーワード: cytokine, neurotrophic factor, growth factor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86502.89

構造登録者

Mcdonald, N.Q.,Panayotatos, N.,Hendrickson, W.A. (登録日: 1996-06-06, 公開日: 1997-03-26, 最終更新日: 2024-02-07)

主引用文献

McDonald, N.Q.,Panayotatos, N.,Hendrickson, W.A.
Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing.
EMBO J., 14:2689-2699, 1995

PubMed Abstract: Ciliary neurotrophic factor (CNTF) promotes the survival and differentiation of developing motor neurons and is a potential therapeutic for treating neurodegeneration and nerve injury. The crystal structure of human CNTF has been determined at 2.4 A resolution using multi-wavelength anomalous diffraction (MAD) phasing from a single Yb3+ ions. The structure reveals that CNTF is dimeric, with a novel anti-parallel arrangement of the subunits, not previously observed for other cytokines. Each subunit adopts a double crossover four-helix bundle fold, in which two helices contribute to the dimer interface, whilst two different helices show pronounced kinks. Analysis of the electrostatic surface of CNTF identified residues within these kinked helices that may contact the CNTF receptor-alpha. Solution experiments show that CNTF dimerizes at concentrations > 40 microM. Such dimers are likely to be relevant to the storage of CNTF in the peripheral nerve given the high concentrations present in this tissue. However, it is unlikely that they play a role in engaging the three distinct receptor subunits that comprise the CNTF receptor, given the low concentration of extracellular CNTF and its high potency.

PubMed: 7796798

実験手法

X-RAY DIFFRACTION (2.4 Å)