Article Metrics


Online attention

Structural Analysis Uncovers Lipid-Binding Properties of Notch Ligands

DOI: 10.1016/j.celrep.2013.10.029 DOI Help
PMID: 24239355 PMID Help

Authors: Chandramouli r. Chillakuri (University of Oxford) , Devon Sheppard (University of Oxford) , Ma. xenia g. Ilagan (Washington University School of Medicine) , Laurie r. Holt (University of Oxford) , Felicity Abbott (University of Oxford) , Shaoyan Liang (University of Oxford) , Raphael Kopan (Washington University School of Medicine) , Penny a. Handford (University of Oxford) , Susan Lea (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell Reports , VOL 5 (4) , PAGES 861 - 867

State: Published (Approved)
Published: November 2013

Abstract: Notch ligands contain an N-terminal C2 phospholipid recognition domain Ca2+-dependent lipid binding by Jagged 1 is required for optimal Notch activation Lipid binding by Notch ligands is calcium dependent Notch ligands require bound calcium at the N terminus for full activity

Journal Keywords: Calcium; Calcium-Binding; Cell; Cell; Crystallography; X-Ray; Enzyme; Fatty; HEK293; Humans; Intercellular; Membrane; Molecular; Phospholipids; Protein; Tertiary; Receptors; Notch; Sequence; Signal Transduction

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 18/12/2013 09:59

Discipline Tags:

Technical Tags: