4WMV

STRUCTURE OF MBP-MCL1 BOUND TO ligand 4 AT 2.4A

4WMV の概要

• エントリーDOI: 10.2210/pdb4wmv/pdb
• 関連するPDBエントリー: 4WMR 4WMS 4WMT 4WMU 4WMW 4WMX
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: MBL-MCL1 chimera protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: apoptosis, protein-protein interaction
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57943.58

構造登録者

Clifton, M.C.,Moulin, A. (登録日: 2014-10-09, 公開日: 2015-05-06, 最終更新日: 2023-09-27)

主引用文献

Clifton, M.C.,Dranow, D.M.,Leed, A.,Fulroth, B.,Fairman, J.W.,Abendroth, J.,Atkins, K.A.,Wallace, E.,Fan, D.,Xu, G.,Ni, Z.J.,Daniels, D.,Van Drie, J.,Wei, G.,Burgin, A.B.,Golub, T.R.,Hubbard, B.K.,Serrano-Wu, M.H.
A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.
Plos One, 10:e0125010-e0125010, 2015

PubMed Abstract: Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.

PubMed: 25909780
DOI: 10.1371/journal.pone.0125010

実験手法

X-RAY DIFFRACTION (2.4 Å)