2A4J

Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a 17 residues peptide (P1-XPC) from xeroderma pigmentosum group C protein

「1T2G」から置き換えられました

2A4J の概要

• エントリーDOI: 10.2210/pdb2a4j/pdb
• NMR情報: BMRB: 5992
• 分子名称: Centrin 2, 17-mer peptide P1-XPC from DNA-repair protein complementing XP-C cells (2 entities in total)
• 機能のキーワード: ef-hand, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, centrosome, centriole: P41208; Nucleus: Q96AX0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11347.96

構造登録者

Yang, A.,Miron, S.,Mouawad, L.,Duchambon, P.,Blouquit, Y.,Craescu, C.T. (登録日: 2005-06-29, 公開日: 2005-07-12, 最終更新日: 2024-05-22)

主引用文献

Yang, A.,Miron, S.,Mouawad, L.,Duchambon, P.,Blouquit, Y.,Craescu, C.T.
Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair.
Biochemistry, 45:3653-3663, 2006

PubMed Abstract: Human centrin 2 is a component of the nucleotide excision repair system, as a subunit of the heterotrimer including xeroderma pigmentosum group C protein (XPC) and hHR23B. The C-terminal domain of centrin (C-HsCen2) binds strongly a peptide from the XPC protein (P1-XPC: N(847)-R(863)). Here, we characterize the solution Ca(2+)-dependent structural and molecular features of the C-HsCen2 in complex with P1-XPC, mainly using NMR spectroscopy and molecular modeling. The N-terminal half of the peptide, organized as an alpha helix is anchored into a deep hydrophobic cavity of the protein, because of three bulky hydrophobic residues in position 1-4-8 and electrostatic contacts with the centrin helix E. Investigation of the whole centrin interactions shows that the N-terminal domain of the protein is not involved in the complex formation and is structurally independent from the peptide-bound C-terminal domain. The complex may exist in three different binding conformations corresponding to zero, one, and two Ca(2+)-bound states, which may exchange with various rates and have distinct structural stability. The various features of the intermolecular interaction presented here constitute a centrin-specific mode for the target binding.

PubMed: 16533048
DOI: 10.1021/bi0524868

実験手法

SOLUTION NMR