PDBsum entry 1v2h

Transferase

PDB id: 1v2h

Contents

Protein chain

288 a.a. *

Ligands

SO4 ×4

GUN

Waters ×38

* Residue conservation analysis

PDB id:

1v2h

Name:

Transferase

Title:

Crystal structure of human pnp complexed with guanine

Structure:

Purine nucleoside phosphorylase. Chain: e. Synonym: inosine phosphorylase, pnp. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: pnp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PDB file)

Resolution:

2.70Å R-factor: 0.218 R-free: 0.293

Authors:

W.F.De Azevedo Jr.,F.Canduri,J.H.Pereira,D.M.Dos Santos,M.V.Bertacine Dias,R.G.Silva,M.S.Palma,L.A.Basso,D.S.Santos

Key ref:

W.F.de Azevedo et al. (2003). Crystal structure of human PNP complexed with guanine. Biochem Biophys Res Commun, 312, 767-772. PubMed id: 14680831 DOI: 10.1016/j.bbrc.2003.10.190

Date:

16-Oct-03 Release date: 13-Jan-04

Protein chain

P00491  (PNPH_HUMAN) -  Purine nucleoside phosphorylase from Homo sapiens

Seq: 289 a.a.

Struc: 288 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.2.4.2.1 - purine-nucleoside phosphorylase.
• Reaction:
  1. a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha- D-ribose 1-phosphate
  2. a purine 2'-deoxy-D-ribonucleoside + phosphate = a purine nucleobase + 2-deoxy-alpha-D-ribose 1-phosphate

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

reference

DOI no: 10.1016/j.bbrc.2003.10.190

Biochem Biophys Res Commun 312:767-772 (2003)

PubMed id: 14680831

Crystal structure of human PNP complexed with guanine.

W.F.de Azevedo, F.Canduri, D.M.dos Santos, J.H.Pereira, M.V.Bertacine Dias, R.G.Silva, M.A.Mendes, L.A.Basso, M.S.Palma, D.S.Santos.

ABSTRACT

Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. PNP is a target for inhibitor development aiming at T-cell immune response modulation and has been submitted to extensive structure-based drug design. More recently, the 3-D structure of human PNP has been refined to 2.3A resolution, which allowed a redefinition of the residues involved in the substrate-binding sites and provided a more reliable model for structure-based design of inhibitors. This work reports crystallographic study of the complex of Human PNP:guanine (HsPNP:Gua) solved at 2.7A resolution using synchrotron radiation. Analysis of the structural differences among the HsPNP:Gua complex, PNP apoenzyme, and HsPNP:immucillin-H provides explanation for inhibitor binding, refines the purine-binding site, and can be used for future inhibitor design.