PDBsum entry 4zqk

Immune system

PDB id: 4zqk

Contents

Protein chains

115 a.a.

106 a.a.

Metals

_NA

Waters ×15

PDB id:

4zqk

Name:

Immune system

Title:

Structure of the complex of human programmed death-1 (pd-1) and its ligand pd-l1.

Structure:

Programmed cell death 1 ligand 1. Chain: a. Synonym: programmed death ligand 1,b7 homolog 1,b7-h1. Engineered: yes. Programmed cell death protein 1. Chain: b. Fragment: unp residues 33-150. Synonym: hpd-1. Engineered: yes.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cd274, b7h1, pdcd1l1, pdcd1lg1, pdl1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: pdcd1, pd1. Expression_system_taxid: 469008

Resolution:

2.45Å R-factor: 0.209 R-free: 0.253

Authors:

K.M.Zak,G.Dubin,T.A.Holak

Key ref:

K.M.Zak et al. (2015). Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1. Structure, 23, 2341-2348. PubMed id: 26602187 DOI: 10.1016/j.str.2015.09.010

Date:

10-May-15 Release date: 04-Nov-15

Protein chain

Q9NZQ7  (PD1L1_HUMAN) -  Programmed cell death 1 ligand 1 from Homo sapiens

Seq: 290 a.a.

Struc: 115 a.a.

Protein chain

Q15116  (PDCD1_HUMAN) -  Programmed cell death protein 1 from Homo sapiens

Seq: 288 a.a.

Struc: 106 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.str.2015.09.010

Structure 23:2341-2348 (2015)

PubMed id: 26602187

Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1.

K.M.Zak, R.Kitel, S.Przetocka, P.Golik, K.Guzik, B.Musielak, A.Dömling, G.Dubin, T.A.Holak.

ABSTRACT

Targeting the PD-1/PD-L1 immunologic checkpoint with monoclonal antibodies has recently provided breakthrough progress in the treatment of melanoma, non-small cell lung cancer, and other types of cancer. Small-molecule drugs interfering with this pathway are highly awaited, but their development is hindered by insufficient structural information. This study reveals the molecular details of the human PD-1/PD-L1 interaction based on an X-ray structure of the complex. First, it is shown that the ligand binding to human PD-1 is associated with significant plasticity within the receptor. Second, a detailed molecular map of the interaction surface is provided, allowing definition of the regions within both interacting partners that may likely be targeted by small molecules.