2M1S

NMR assignment of the arenaviral protein Z from Lassa fever virus

「2KO5」から置き換えられました

2M1S の概要

• エントリーDOI: 10.2210/pdb2m1s/pdb
• NMR情報: BMRB: 15660
• 分子名称: RING finger protein Z, ZINC ION (2 entities in total)
• 機能のキーワード: ring, negative regulator of eif4e, transcription
• 由来する生物種: Lassa virus Josiah
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10819.25

構造登録者

Volpon, L.,Osborne, M.J.,Borden, K.L.B. (登録日: 2012-12-06, 公開日: 2013-01-30, 最終更新日: 2024-05-15)

主引用文献

Volpon, L.,Osborne, M.J.,Capul, A.A.,de la Torre, J.C.,Borden, K.L.B.
Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E
Proc.Natl.Acad.Sci.USA, 107:5441-5446, 2010

PubMed Abstract: The eukaryotic translation initiation factor eIF4E, a potent oncogene, is highly regulated. One class of eIF4E regulators, including eIF4G and the 4E-binding proteins (4E-BPs), interact with eIF4E using a conserved YXXXXLPhi-binding site. The structural basis of this interaction and its regulation are well established. Really Interesting New Gene (RING) domain containing proteins, such as the promyelocytic leukemia protein PML and the arenaviral protein Z, represent a second class of eIF4E regulators that inhibit eIF4E function by decreasing eIF4E's affinity for its m(7)G cap ligand. To elucidate the structural basis of this inhibition, we determined the structure of Z and studied the Z-eIF4E complex using NMR methods. We show that Z interacts with eIF4E via a novel binding site, which has no homology with that of eIF4G or the 4E-BPs, and is different from the RING recognition site used in the ubiquitin system. Z and eIF4G interact with distinct parts of eIF4E and differentially alter the conformation of the m(7)G cap-binding site. Our results provide a molecular basis for how PML and Z RINGs reduce the affinity of eIF4E for the m(7)G cap and thereby act as key inhibitors of eIF4E function. Furthermore, our findings provide unique insights into RING protein interactions.

PubMed: 20212144
DOI: 10.1073/pnas.0909877107

実験手法

SOLUTION NMR