Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.

doi:10.1002/prot.340150110

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Article

Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.

Proteins - 1 Jan 1993

Xue Y, Vidgren J, Svensson L A, Liljas A, Jonsson B H, Lindskog S

Abstract excerpt

A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was mutated at position 200 from threonine to histidine, which results in higher affinity for bicarbonate. The HCO3- ion binds in the active site to the zinc ion...

Topics

Bicarbonates
Carbonic Anhydrases
Crystallization
Humans
Hydrogen Bonding
Mathematical Computing
Models, Molecular
Mutation
Protein Conformation
X-Ray Diffraction
Zinc

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