Document Detail


Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-{beta}-glucosidase mutant that causes Gaucher disease.
MedLine Citation:
PMID:  21724649     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Recently, two studies were published that examined the structure of the acid-β-glucosidase N370S mutant, the most common mutant that causes Gaucher disease. One study used the experimental tool of X-ray crystallography, and the other utilized molecular dynamics (MD). The two studies reinforced each other through the similarities in their findings, but each approach also added some unique information. Both studies report that the conformation of active site loop 3 changes, due to an altered hydrogen bonding network; however, the MD study produced additional data concerning the flexibility of loop 1 and the catalytic residues that are not observed in the other study.
Authors:
Marc N Offman; Marcin Krol; Burkhard Rost; Israel Silman; Joel L Sussman; Anthony H Futerman
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-7-1
Journal Detail:
Title:  Protein engineering, design & selection : PEDS     Volume:  -     ISSN:  1741-0134     ISO Abbreviation:  -     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-7-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101186484     Medline TA:  Protein Eng Des Sel     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Institut für Informatik/I12, Technische Universität München, Boltzmannstr 3, 85748 Garching b. München, Germany.
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