Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
2000-8-29
pubmed:databankReference
pubmed:abstractText
The crystallographic structure of the complex between human aldose reductase (AR2) and one of its inhibitors, IDD384, has been solved at 1.7 A resolution from crystals obtained at pH 5.0. This structure shows that the binding of the inhibitor's hydrophilic head to the catalytic residues Tyr48 and His110 differs from that found previously with porcine AR2. The difference is attributed to a change in the protonation state of the inhibitor (pK(a) = 4.52) when soaked with crystals of human (at pH 5.0) or pig lens AR2 (at pH 6.2). This work demonstrates how strongly the detailed binding of the inhibitor's polar head depends on its protonation state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
536-40
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The structure of human aldose reductase bound to the inhibitor IDD384.
pubmed:affiliation
UPR de Biologie Structurale 9004, IGBMC, CNRS/INSERM/ULP, 1 Rue Laurent Fries, BP 163, 67404 Illkirch, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't