PDBsum entry 3wsj

Hydrolase/hydrolase inhibitor

PDB id: 3wsj

Contents

Protein chains

116 a.a.

Ligands

MK1

SO4 ×13

PG4

Waters ×68

PDB id:

3wsj

Name:

Hydrolase/hydrolase inhibitor

Title:

Htlv-1 protease in complex with the HIV-1 protease inhibitor indinavir

Structure:

Protease. Chain: a, b. Fragment: unp residues 1-116. Engineered: yes. Mutation: yes

Source:

Human t-lymphotropic virus 1. Organism_taxid: 11908. Gene: prt. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.209 R-free: 0.256

Authors:

M.Kuhnert,H.Steuber,W.E.Diederich

Key ref:

M.Kuhnert et al. (2014). Structural basis for HTLV-1 protease inhibition by the HIV-1 protease inhibitor indinavir. J Med Chem, 57, 6266-6272. PubMed id: 25006983 DOI: 10.1021/jm500402c

Date:

14-Mar-14 Release date: 22-Oct-14

Protein chains

Q82134  (Q82134_9DELA) -  Protease (Fragment) from Human T-cell leukemia virus type I

Seq: 125 a.a.

Struc: 116 a.a.*

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

DOI no: 10.1021/jm500402c

J Med Chem 57:6266-6272 (2014)

PubMed id: 25006983

Structural basis for HTLV-1 protease inhibition by the HIV-1 protease inhibitor indinavir.

M.Kuhnert, H.Steuber, W.E.Diederich.

ABSTRACT

HTLV-1 protease (HTLV-1 PR) is an aspartic protease which represents a promising drug target for the discovery of novel anti-HTLV-1 drugs. The X-ray structure of HTLV-1 PR in complex with the well-known and approved HIV-1 PR inhibitor Indinavir was determined at 2.40 Å resolution. In this contribution, we describe the first crystal structure in complex with a nonpeptidic inhibitor that accounts for rationalizing the rather moderate affinity of Indinavir against HTLV-1 PR and provides the basis for further structure-guided optimization strategies.