3LRU

hPRP8 Non-Native Subdomain

3LRU の概要

• エントリーDOI: 10.2210/pdb3lru/pdb
• 分子名称: Pre-mRNA-processing-splicing factor 8 (2 entities in total)
• 機能のキーワード: alternate folding of protein, disease mutation, mrna processing, mrna splicing, nucleus, phosphoprotein, retinitis pigmentosa, ribonucleoprotein, rna-binding, sensory transduction, spliceosome, vision, rna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus speckle : Q6P2Q9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36881.32

構造登録者

Schellenberg, M.J.,Ritchie, D.B.,MacMillan, A.M. (登録日: 2010-02-11, 公開日: 2010-08-25, 最終更新日: 2024-02-21)

主引用文献

Schellenberg, M.J.,Ritchie, D.B.,Wu, T.,Markin, C.J.,Spyracopoulos, L.,MacMillan, A.M.
Context-dependent remodeling of structure in two large protein fragments.
J.Mol.Biol., 402:720-730, 2010

PubMed Abstract: Protein folding involves the formation of secondary structural elements from the primary sequence and their association with tertiary assemblies. The relation of this primary sequence to a specific folded protein structure remains a central question in structural biology. An increasing body of evidence suggests that variations in homologous sequence ranging from point mutations to substantial insertions or deletions can yield stable proteins with markedly different folds. Here we report the structural characterization of domain IV (D4) and ΔD4 (polypeptides with 222 and 160 amino acids, respectively) that differ by virtue of an N-terminal deletion of 62 amino acids (28% of the overall D4 sequence). The high-resolution crystal structures of the monomeric D4 and the dimeric ΔD4 reveal substantially different folds despite an overall conservation of secondary structure. These structures show that the formation of tertiary structures, even in extended polypeptide sequences, can be highly context dependent, and they serve as a model for structural plasticity in protein isoforms.

PubMed: 20713060
DOI: 10.1016/j.jmb.2010.08.020

実験手法

X-RAY DIFFRACTION (1.85 Å)