Linked Life Data

8230097

Source:http://linkedlifedata.com/resource/pubmed/id/8230097

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1993-11-26
pubmed:abstractText
The binding modes of a series of penicillin-derived C2 symmetric dimer inhibitors of HIV-1 proteinase were investigated by NMR, protein crystallography, and molecular modeling. The compounds were found to bind in a symmetrical fashion, tracing and S-shaped course through the active site, with good hydrophobic interactions in the S1/S1' and S2/S2' pockets and hydrogen bonding of inhibitor amide groups. Interactions with the catalytic aspartates appeared poor and the protein conformation was very similar to that seen in complexes with peptidomimetics, in spite of the major differences in ligand structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3113-9
pubmed:dateRevised
2001-11-13
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
A series of penicillin-derived C2-symmetric inhibitors of HIV-1 proteinase: structural and modeling studies.
pubmed:affiliation
Protein Structure Group, Glaxo Group Research Limited, Greenford, Middlesex, United Kingdom.
pubmed:publicationType
Journal Article