PDBsum entry 4xl1

Protein binding

PDB id: 4xl1

Contents

Protein chains

115 a.a.

227 a.a.

Ligands

NAG-NAG ×2

BGC ×6

FUC ×2

NAG ×4

Metals

_CA ×6

Waters ×325

PDB id:

4xl1

Name:

Protein binding

Title:

Complex of notch1 (egf11-13) bound to delta-like 4 (n-egf1)

Structure:

Neurogenic locus notch homolog protein 1. Chain: a, d. Synonym: notch 1. Engineered: yes. Delta-like protein. Chain: b, e. Engineered: yes. Mutation: yes. Other_details: methylated in vitro

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: notch1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hi-five. Gene: dll4, dll4_predicted, rcg_26804.

Resolution:

2.30Å R-factor: 0.220 R-free: 0.259

Authors:

V.C.Luca,K.M.Jude,K.C.Garcia

Key ref:

V.C.Luca et al. (2015). Structural biology. Structural basis for Notch1 engagement of Delta-like 4. Science, 347, 847-853. PubMed id: 25700513 DOI: 10.1126/science.1261093

Date:

13-Jan-15 Release date: 04-Mar-15

Protein chains

Q07008  (NOTC1_RAT) -  Neurogenic locus notch homolog protein 1 from Rattus norvegicus

Seq: 2531 a.a.

Struc: 115 a.a.*

Protein chains

D3ZHH1  (DLL4_RAT) -  Delta-like protein 4 from Rattus norvegicus

Seq: 686 a.a.

Struc: 227 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1126/science.1261093

Science 347:847-853 (2015)

PubMed id: 25700513

Structural biology. Structural basis for Notch1 engagement of Delta-like 4.

V.C.Luca, K.M.Jude, N.W.Pierce, M.V.Nachury, S.Fischer, K.C.Garcia.

ABSTRACT

Notch receptors guide mammalian cell fate decisions by engaging the proteins Jagged and Delta-like (DLL). The 2.3 angstrom resolution crystal structure of the interacting regions of the Notch1-DLL4 complex reveals a two-site, antiparallel binding orientation assisted by Notch1 O-linked glycosylation. Notch1 epidermal growth factor-like repeats 11 and 12 interact with the DLL4 Delta/Serrate/Lag-2 (DSL) domain and module at the N-terminus of Notch ligands (MNNL) domains, respectively. Threonine and serine residues on Notch1 are functionalized with O-fucose and O-glucose, which act as surrogate amino acids by making specific, and essential, contacts to residues on DLL4. The elucidation of a direct chemical role for O-glycans in Notch1 ligand engagement demonstrates how, by relying on posttranslational modifications of their ligand binding sites, Notch proteins have linked their functional capacity to developmentally regulated biosynthetic pathways.