Literature summary for 1.1.1.205 extracted from

Macpherson, I.S.; Kirubakaran, S.; Gorla, S.K.; Riera, T.V.; DAquino, J.A.; Zhang, M.; Cuny, G.D.; Hedstrom, L.
The structural basis of Cryptosporidium-specific IMP dehydrogenase inhibitor selectivity (2010), J. Am. Chem. Soc., 132, 1230-1231.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Cryptosporidium parvum

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion method, to 3.2 A resolution, space group P21212. In complex with inhibitor N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide, to 2.8 A resolution. The thiazole ring of the inhibitor stacks against the purine ring of IMP perpendicularly, and the remainder of the inhibitor extends across the subunit interface into a pocket in the adjacent monomer, where the bromoaniline moiety interacts with Tyr358 from the adjacent subunit. This residue forms a hydrogen-bonding network involving Glu329, Ser354, Thr221, and possibly the amide nitrogen of N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide. Residues Ser22, Pro26, Gly357 of the adjacent subunit and Ala165 form the remainder of the inhibitor binding pocket. With the exception of Thr221, all of these residues are different in human IMPDHs	Cryptosporidium parvum

Crystallization (Comment)

Organism

hanging drop vapour diffusion method, to 3.2 A resolution, space group P21212. In complex with inhibitor N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide, to 2.8 A resolution. The thiazole ring of the inhibitor stacks against the purine ring of IMP perpendicularly, and the remainder of the inhibitor extends across the subunit interface into a pocket in the adjacent monomer, where the bromoaniline moiety interacts with Tyr358 from the adjacent subunit. This residue forms a hydrogen-bonding network involving Glu329, Ser354, Thr221, and possibly the amide nitrogen of N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide. Residues Ser22, Pro26, Gly357 of the adjacent subunit and Ala165 form the remainder of the inhibitor binding pocket. With the exception of Thr221, all of these residues are different in human IMPDHs

Cryptosporidium parvum

Inhibitors

Inhibitors	Comment	Organism
N-(2,3-dichlorophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide	poor inhibition of human IMPDH2	Cryptosporidium parvum
N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide	crystallization data. Poor inhibition of human IMPDH2	Cryptosporidium parvum
N-(naphthalen-2-yl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide	poor inhibition of human IMPDH2	Cryptosporidium parvum
N-(naphthalen-2-yl)-2-[2-(1,3-thiazol-4-yl)-1H-benzimidazol-1-yl]acetamide	poor inhibition of human IMPDH2	Cryptosporidium parvum

Organism

Organism	UniProt	Comment	Textmining
Cryptosporidium parvum	Q8T6T2	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombnant enzyme	Cryptosporidium parvum

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor
0.000007	-	pH not specified in the publication, temperature not specified in the publication	Cryptosporidium parvum	N-(naphthalen-2-yl)-2-[2-(1,3-thiazol-4-yl)-1H-benzimidazol-1-yl]acetamide
0.000008	-	pH not specified in the publication, temperature not specified in the publication	Cryptosporidium parvum	N-(naphthalen-2-yl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide
0.000018	-	pH not specified in the publication, temperature not specified in the publication	Cryptosporidium parvum	N-(2,3-dichlorophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide
0.000028	-	pH not specified in the publication, temperature not specified in the publication	Cryptosporidium parvum	N-(4-bromophenyl)-2-[2-(1,3-thiazol-2-yl)-1H-benzimidazol-1-yl]acetamide