4AYA

Crystal structure of ID2 HLH homodimer at 2.1A resolution

4AYA の概要

• エントリーDOI: 10.2210/pdb4aya/pdb
• 分子名称: DNA-BINDING PROTEIN INHIBITOR ID-2, POTASSIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: cell cycle
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm (By similarity): Q02363
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21826.37

構造登録者

Wong, M.V.,Jiang, S.,Palasingam, P.,Kolatkar, P.R. (登録日: 2012-06-19, 公開日: 2012-11-14, 最終更新日: 2024-05-01)

主引用文献

Wong, M.V.,Jiang, S.,Palasingam, P.,Kolatkar, P.R.
A Divalent Ion is Crucial in the Structure and Dominant-Negative Function of Id Proteins, a Class of Helix-Loop-Helix Transcription Regulators.
Plos One, 7:48591-, 2012

PubMed Abstract: Inhibitors of DNA binding and differentiation (ID) proteins, a dominant-negative group of helix-loop-helix (HLH) transcription regulators, are well-characterized key players in cellular fate determination during development in mammals as well as Drosophila. Although not oncogenes themselves, their upregulation by various oncogenic proteins (such as Ras, Myc) and their inhibitory effects on cell cycle proteins (such as pRb) hint at their possible roles in tumorigenesis. Furthermore, their potency as inhibitors of cellular differentiation, through their heterodimerization with subsequent inactivation of the ubiquitous E proteins, suggest possible novel roles in engineering induced pluripotent stem cells (iPSCs). We present the high-resolution 2.1Å crystal structure of ID2 (HLH domain), coupled with novel biochemical insights in the presence of a divalent ion, possibly calcium (Ca2+), in the loop of ID proteins, which appear to be crucial for the structure and activity of ID proteins. These new insights will pave the way for new rational drug designs, in addition to current synthetic peptide options, against this potent player in tumorigenesis as well as more efficient ways for stem cells reprogramming.

PubMed: 23119064
DOI: 10.1371/JOURNAL.PONE.0048591

実験手法

X-RAY DIFFRACTION (2.103 Å)