A_amylase_inhib | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a | |||||||||
Identifiers | |||||||||
Symbol | A_amylase_inhib | ||||||||
Pfam | PF01356 | ||||||||
InterPro | IPR000833 | ||||||||
SCOP2 | 1hoe / SCOPe / SUPFAM | ||||||||
|
Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases.
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. [1] The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity.
More information about this protein can be found at Protein of the Month: alpha-Amylase .
{{
cite journal}}
: CS1 maint: date and year (
link) CS1 maint: multiple names: authors list (
link)
A_amylase_inhib | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a | |||||||||
Identifiers | |||||||||
Symbol | A_amylase_inhib | ||||||||
Pfam | PF01356 | ||||||||
InterPro | IPR000833 | ||||||||
SCOP2 | 1hoe / SCOPe / SUPFAM | ||||||||
|
Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases.
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. [1] The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity.
More information about this protein can be found at Protein of the Month: alpha-Amylase .
{{
cite journal}}
: CS1 maint: date and year (
link) CS1 maint: multiple names: authors list (
link)