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| {{STRUCTURE_2fak| PDB=2fak | SCENE= }} | | {{STRUCTURE_2fak| PDB=2fak | SCENE= }} |
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| '''Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome'''
| | ===Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome=== |
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| ==Overview==
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| The crystal structures of the yeast 20S proteasome core particle (CP) in complex with Salinosporamides A (NPI-0052; 1) and B (4) were solved at <3 angstroms resolution. Each ligand is covalently bound to Thr1O(gamma) via an ester linkage to the carbonyl derived from the beta-lactone ring of the inhibitor. In the case of 1, nucleophilic addition to the beta-lactone ring is followed by addition of C-3O to the chloroethyl group, giving rise to a cyclic ether. The crystal structures were compared to that of the omuralide/CP structure solved previously, and the collective data provide new insights into the mechanism of inhibition and irreversible binding of 1. Upon opening of the beta-lactone ring, C-3O assumes the position occupied by a water molecule in the unligated enzyme and hinders deacylation of the enzyme-ligand complex. Furthermore, the resulting protonation state of Thr1NH2 deactivates the catalytic N-terminus. | | The line below this paragraph, {{ABSTRACT_PUBMED_16608349}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16608349 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16608349}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Proteasome]] | | [[Category: Proteasome]] |
| [[Category: Ubiquitin]] | | [[Category: Ubiquitin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:39:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:12:51 2008'' |