Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6378
pubmed:dateCreated
1992-7-21
pubmed:abstractText
X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
466-72
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1608447-Amino Acid Sequence, pubmed-meshheading:1608447-Animals, pubmed-meshheading:1608447-Binding Sites, pubmed-meshheading:1608447-Chemistry, Physical, pubmed-meshheading:1608447-Crystallization, pubmed-meshheading:1608447-Drug Design, pubmed-meshheading:1608447-Humans, pubmed-meshheading:1608447-Hydrogen Bonding, pubmed-meshheading:1608447-Mice, pubmed-meshheading:1608447-Molecular Sequence Data, pubmed-meshheading:1608447-Molecular Structure, pubmed-meshheading:1608447-Oligopeptides, pubmed-meshheading:1608447-Physicochemical Phenomena, pubmed-meshheading:1608447-Protease Inhibitors, pubmed-meshheading:1608447-Protein Binding, pubmed-meshheading:1608447-Protein Conformation, pubmed-meshheading:1608447-Renin, pubmed-meshheading:1608447-Substrate Specificity, pubmed-meshheading:1608447-X-Ray Diffraction
pubmed:year
1992
pubmed:articleTitle
X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.
pubmed:affiliation
Department of Crystallography, Birkbeck College, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't