PDBsum entry 5l04

Transferase/transferase inhibitor

PDB id: 5l04

Contents

Protein chains

460 a.a.

37 a.a.

Waters ×185

PDB id:

5l04

Name:

Transferase/transferase inhibitor

Title:

Structure of interferon lambda 1 receptor with human kinase jak1

Structure:

Tyrosine-protein kinase jak1. Chain: a. Fragment: unp residues 31-577. Synonym: janus kinase 1,jak-1. Engineered: yes. Interferon lambda receptor 1. Chain: b. Fragment: unp residues 260-307. Synonym: ifn-lambda-r1,cytokine receptor class-ii member 12,cytokine

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: jak1, jak1a, jak1b. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: rosetta 2 (de3). Gene: ifnlr1, il28ra, licr2.

Resolution:

2.10Å R-factor: 0.171 R-free: 0.230

Authors:

J.Lubkowski,A.Wlodawer,D.Zhang

Key ref:

D.Zhang et al. (2016). Crystal Structure of a Complex of the Intracellular Domain of Interferon λ Receptor 1 (IFNLR1) and the FERM/SH2 Domains of Human JAK1. J Mol Biol, 428, 4651-4668. PubMed id: 27725180 DOI: 10.1016/j.jmb.2016.10.005

Date:

26-Jul-16 Release date: 12-Oct-16

Protein chain

P23458  (JAK1_HUMAN) -  Tyrosine-protein kinase JAK1 from Homo sapiens

Seq: 1154 a.a.

Struc: 460 a.a.

Protein chain

Q8IU57  (INLR1_HUMAN) -  Interferon lambda receptor 1 from Homo sapiens

Seq: 520 a.a.

Struc: 37 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.10.2 - non-specific protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.jmb.2016.10.005

J Mol Biol 428:4651-4668 (2016)

PubMed id: 27725180

Crystal Structure of a Complex of the Intracellular Domain of Interferon λ Receptor 1 (IFNLR1) and the FERM/SH2 Domains of Human JAK1.

D.Zhang, A.Wlodawer, J.Lubkowski.

ABSTRACT

The crystal structure of a construct consisting of the FERM and SH2-like domains of the human Janus kinase 1 (JAK1) bound to a fragment of the intracellular domain of the interferon-λ receptor 1 (IFNLR1) has been determined at the nominal resolution of 2.1Å. In this structure, the receptor peptide forms an 85-Å-long extended chain, in which both the previously identified box1 and box2 regions bind simultaneously to the FERM and SH2-like domains of JAK1. Both domains of JAK1 are generally well ordered, with regions not seen in the crystal structure limited to loops located away from the receptor-binding regions. The structure provides a much more complete and accurate picture of the interactions between JAK1 and IFNLR1 than those given in earlier reports, illuminating the molecular basis of the JAK-cytokine receptor association. A glutamate residue adjacent to the box2 region in IFNLR1 mimics the mode of binding of a phosphotyrosine in classical SH2 domains. It was shown here that a deletion of residues within the box1 region of the receptor abolishes stable interactions with JAK1, although it was previously shown that box2 alone is sufficient to stabilize a similar complex of the interferon-α receptor and TYK2.