1u33
From Proteopedia
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|PDB= 1u33 |SIZE=350|CAPTION= <scene name='initialview01'>1u33</scene>, resolution 1.95Å | |PDB= 1u33 |SIZE=350|CAPTION= <scene name='initialview01'>1u33</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=LM2:4 | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=LM2:4'-O-METHYL-MALTOSYL-ALPHA+(1,4)-(Z,+3S,4S,5R,6R)-3,4,5-TRIHYDROXY-6-HYDROXYMETHYL-PIPERIDIN-2-ONE'>LM2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] | ||
|GENE= AMY2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= AMY2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
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[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:49:20 2008'' |
Revision as of 11:49, 23 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | AMY2A (Homo sapiens) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
In situ extension as an approach for identifying novel alpha-amylase inhibitors
Overview
A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K(i) value of 18 mm to a trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.
About this Structure
1U33 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
In situ extension as an approach for identifying novel alpha-amylase inhibitors., Numao S, Damager I, Li C, Wrodnigg TM, Begum A, Overall CM, Brayer GD, Withers SG, J Biol Chem. 2004 Nov 12;279(46):48282-91. Epub 2004 Aug 10. PMID:15304511
Page seeded by OCA on Sun Mar 23 13:49:20 2008
Categories: Alpha-amylase | Homo sapiens | Single protein | Begum, A. | Brayer, G D. | Damager, I. | Li, C. | Numao, S. | Overall, C M. | Withers, S G. | Wrodnigg, T M. | CA | CL | LM2 | NAG | Acarbose | Enzyme mechanism | Glucosidase | Glycosidase | Human pancreatic alpha-amylase | Inhibitor
