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| - | [[Image:1dhk.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1dhk| PDB=1dhk | SCENE= }} | | {{STRUCTURE_1dhk| PDB=1dhk | SCENE= }} |
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| - | '''STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE'''
| + | ===STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE=== |
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| - | ==Overview==
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| - | BACKGROUND: alpha-Amylases catalyze the hydrolysis of glycosidic linkages in starch and other related polysaccharides. The alpha-amylase inhibitor (alpha-Al) from the bean Phaseolus vulgaris belongs to a family of plant defence proteins and is a potent inhibitor of mammalian alpha-amylases. The structure of pig pancreatic alpha-amylase (PPA) in complex with both a carbohydrate inhibitor (acarbose) and a proteinaceous inhibitor (Tendamistat) is known, but the catalytic mechanism is poorly understood. RESULTS: The crystal structure of pig pancreatic alpha-amylase complexed with alpha-Al was refined to 1.85 A resolution. It reveals that in complex with PPA, the inhibitor has the typical dimer structure common to legume lectins. Two hairpin loops extending out from the jellyroll fold of a monomer interact directly with the active site region of the enzyme molecule, with the inhibitor molecule filling the whole substrate-docking region of the PPA. The inhibitor makes substrate-mimetic interactions with binding subsites of the enzyme and targets catalytic residues in the active site. Binding of inhibitor induces structural changes at the active site of the enzyme. CONCLUSIONS: The present analysis reveals that there are extensive interactions between the inhibitor and residues that are highly conserved in the active site of alpha-amylases; alpha-Al1 inactivates PPA through elaborate blockage of substrate-binding sites. It provides a basis to design peptide analogue inhibitors. alpha-Amylase inhibition is of interest from several points of view, for example the treatment of diabetes and for crop protection.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8994970}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8994970 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8994970}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pancreatic alpha-amylase]] | | [[Category: Pancreatic alpha-amylase]] |
| | [[Category: Porcine]] | | [[Category: Porcine]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:04:32 2008'' |
Revision as of 20:04, 30 June 2008
Template:STRUCTURE 1dhk
STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE
Template:ABSTRACT PUBMED 8994970
About this Structure
1DHK is a Protein complex structure of sequences from Phaseolus vulgaris and Sus scrofa. Full crystallographic information is available from OCA.
Reference
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex., Bompard-Gilles C, Rousseau P, Rouge P, Payan F, Structure. 1996 Dec 15;4(12):1441-52. PMID:8994970
Page seeded by OCA on Mon Jun 30 23:04:32 2008
