Target Information
Target General Information | Top | |||||
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Target ID |
T54519
(Former ID: TTDI01929)
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Target Name |
Schistosoma Purine nucleoside phosphorylase (sch PNP)
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Synonyms |
sch Purine nucleoside phosphorylase; sch Inosine-guanosine phosphorylase
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Gene Name |
sch PNP
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Target Type |
Clinical trial target
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[1] | ||||
Disease | [+] 1 Target-related Diseases | + | ||||
1 | Prostate cancer [ICD-11: 2C82] | |||||
Function |
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
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UniProt ID | ||||||
EC Number |
EC 2.4.2.1
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Sequence |
MHESVTANIENVKKVAHHIQKLTSIVPEIGIICGSGLGKLADGVKDKITIPYTKIPNFPQ
TSVVGHSGNLIFGTLSGRKVVVMQGRFHMYEGYSNDTVALPIRVMKLLGVKILMVSNAAG GLNRSLKLGDFVILKDHIYLPGLGLNNILVGPNQEAFGTRFPALSNAYDRDLRKLAVQVA EENGFGNLVHQGVYVMNGGPCYETPAECTMLLNMGCDVVGMSTIPEVVIARHCGIQVFAV SLVTNISVLDVESDLKPNHEEVLATGAQRAELMQSWFEKIIEKLPKD Click to Show/Hide
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3D Structure | Click to Show 3D Structure of This Target | PDB |
Drugs and Modes of Action | Top | |||||
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Clinical Trial Drug(s) | [+] 1 Clinical Trial Drugs | + | ||||
1 | FP-253-GDEPT | Drug Info | Phase 1 | Prostate cancer | [1] | |
Mode of Action | [+] 1 Modes of Action | + | ||||
Modulator | [+] 1 Modulator drugs | + | ||||
1 | FP-253-GDEPT | Drug Info | [1] |
Drug Binding Sites of Target | Top | |||||
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Ligand Name: Adenosine | Ligand Info | |||||
Structure Description | Crystal structure of Schistosoma mansoni purine nucleoside phosphorylase in complex with adenosine | PDB:3F8W | ||||
Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [2] |
PDB Sequence |
SVTANIENVK
13 KVAHHIQKLT23 SIVPEIGIIC33 GSGLGKLADG43 VKDKITIPYT53 KIPNFPQTSH 66 SGNLIFGTLS76 GRKVVVMQGR86 FHMYEGYSND96 TVALPIRVMK106 LLGVKILMVS 116 NAAGGLNRSL126 KLGDFVILKD136 HIYLPGLGLN146 NILVGPNQEA156 FGTRFPALSN 166 AYDRDLRKLA176 VQVAEENGFG186 NLVHQGVYVM196 NGGPCYETPA206 ECTMLLNMGC 216 DVVGMSTIPE226 VVIARHCGIQ236 VFAVSLVTNI246 SVLDVESDLK256 PNHEEVLATG 266 AQRAELMQSW276 FEKIIEKLPK286
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Ligand Name: Guanosine | Ligand Info | |||||
Structure Description | Schistosoma Purine nucleoside phosphorylase in complex with guanosine | PDB:3IEX | ||||
Method | X-ray diffraction | Resolution | 2.05 Å | Mutation | No | [3] |
PDB Sequence |
SVTANIENVK
13 KVAHHIQKLT23 SIVPEIGIIC33 GSGLGGVKDK47 ITIPYTKIPN57 FPQTSSGNLI 71 FGTLSGRKVV81 VMQGRFHMYE91 GYSNDTVALP101 IRVMKLLGVK111 ILMVSNAAGG 121 LNRSLKLGDF131 VILKDHIYLP141 GLGLNNILVG151 PNQEAFGTRF161 PALSNAYDRD 171 LRKLAVQVAE181 ENGFGNLVHQ191 GVYVMNGGPC201 YETPAECTML211 LNMGCDVVGM 221 STIPEVVIAR231 HCGIQVFAVS241 LVTNISVLDV251 ESDLKPNHEE261 VLATGAQRAE 271 LMQSWFEKII281 EKLPKD
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Click to View More Binding Site Information of This Target with Different Ligands |
Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Similarity Proteins
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There is no similarity protein (E value < 0.005) for this target
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References | Top | |||||
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REF 1 | Purine nucleoside phosphorylase and fludarabine phosphate gene-directed enzyme prodrug therapy suppresses primary tumour growth and pseudo-metastases in a mouse model of prostate cancer. J Gene Med. 2004 Dec;6(12):1343-57. | |||||
REF 2 | Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):73-9. | |||||
REF 3 | Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: kinetic and structural studies. Bioorg Med Chem. 2010 Feb 15;18(4):1421-7. |
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