1DDM

SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE

1DDM の概要

• エントリーDOI: 10.2210/pdb1ddm/pdb
• 関連するPDBエントリー: 2NMB
• 分子名称: NUMB PROTEIN, NUMB ASSOCIATE KINASE (2 entities in total)
• 機能のキーワード: complex, signal transduction, phosphotyrosine binding domain (ptb), asymmetric cell division, signaling protein-transferase complex, signaling protein/transferase
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• 細胞内の位置: Nucleus: P16554
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16554.78

構造登録者

Zwahlen, C.,Li, S.C.,Kay, L.E.,Pawson, T.,Forman-Kay, J.D. (登録日: 1999-11-11, 公開日: 2000-04-10, 最終更新日: 2024-05-22)

主引用文献

Zwahlen, C.,Li, S.C.,Kay, L.E.,Pawson, T.,Forman-Kay, J.D.
Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb.
EMBO J., 19:1505-1515, 2000

PubMed Abstract: The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb is involved in the formation of multiple protein complexes in vivo and can bind a diverse array of peptide sequences in vitro. To investigate the structural basis for the promiscuous nature of this protein module, we have determined its solution structure by NMR in a complex with a peptide containing an NMSF sequence derived from the Numb-associated kinase (Nak). The Nak peptide was found to adopt a significantly different structure from that of a GPpY sequence-containing peptide previously determined. In contrast to the helical turn adopted by the GPpY peptide, the Nak peptide forms a beta-turn at the NMSF site followed by another turn near the C-terminus. The Numb PTB domain appears to recognize peptides that differ in both primary and secondary structures by engaging various amounts of the binding surface of the protein. Our results suggest a mechanism through which a single PTB domain might interact with multiple distinct target proteins to control a complex biological process such as asymmetric cell division.

PubMed: 10747019
DOI: 10.1093/emboj/19.7.1505

実験手法

SOLUTION NMR