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PDBsum entry 1v2h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of human pnp complexed with guanine.
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Authors
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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.
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Ref.
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Biochem Biophys Res Commun, 2003,
312,
767-772.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystal structure of human purine nucleoside phosphorylase at 2.3a resolution.
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Authors
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W.F.De azevedo,
F.Canduri,
D.M.Dos santos,
R.G.Silva,
J.S.De oliveira,
L.P.De carvalho,
L.A.Basso,
M.A.Mendes,
M.S.Palma,
D.S.Santos.
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Ref.
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Biochem Biophys Res Commun, 2003,
308,
545-552.
[DOI no: ]
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PubMed id
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