1CMO

IMMUNOGLOBULIN MOTIF DNA-RECOGNITION AND HETERODIMERIZATION FOR THE PEBP2/CBF RUNT-DOMAIN

1CMO の概要

• エントリーDOI: 10.2210/pdb1cmo/pdb
• 分子名称: POLYOMAVIRUS ENHANCER BINDING PROTEIN 2 (1 entity in total)
• 機能のキーワード: transcription factor, hematopoiesis, osteogenesis, ig-fold, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q01196
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14008.94

構造登録者

Nagata, T.,Gupta, V.,Sorce, D.,Kim, W.Y.,Sali, A.,Chait, B.T.,Shigesada, K.,Ito, Y.,Werner, M.H. (登録日: 1999-05-11, 公開日: 2000-01-05, 最終更新日: 2023-12-27)

主引用文献

Nagata, T.,Gupta, V.,Sorce, D.,Kim, W.Y.,Sali, A.,Chait, B.T.,Shigesada, K.,Ito, Y.,Werner, M.H.
Immunoglobulin motif DNA recognition and heterodimerization of the PEBP2/CBF Runt domain.
Nat.Struct.Biol., 6:615-618, 1999

PubMed Abstract: The polyomavirus enhancer binding protein 2 (PEBP2) or core binding factor (CBF) is a heterodimeric enhancer binding protein that is associated with genetic regulation of hematopoiesis and osteogenesis. Aberrant forms of PEBP2/CBF are implicated in the cause of the acute human leukemias and in a disorder of bone development known as cleidocranial dysplasia. The common denominator in the natural and mutant forms of this protein is a highly conserved domain of PEBP2/CBF alpha, termed the Runt domain (RD), which is responsible for both DNA binding and heterodimerization with the beta subunit of PEBP2/CBF. The three-dimensional structure of the RD bound to DNA has been determined to be an S-type immunoglobulin fold, establishing a structural relationship between the RD and the core DNA binding domains of NF-kappaB, NFAT1, p53 and the STAT proteins. NMR spectroscopy of a 43.6 kD RD-beta-DNA ternary complex identified the surface of the RD in contact with the beta subunit, suggesting a mechanism for the enhancement of RD DNA binding by beta. Analysis of leukemogenic mutants within the RD provides molecular insights into the role of this factor in leukemogenesis and cleidocranial dysplasia.

PubMed: 10404214
DOI: 10.1038/10658

実験手法

SOLUTION NMR