Linked Life Data

3801447

Source:http://linkedlifedata.com/resource/pubmed/id/3801447

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1987-3-20
pubmed:abstractText
Band 3 is proposed to contain substrate channels that lead from the aqueous medium to a transport site buried within the membrane, and which can be blocked by inhibitors. The inhibitors 1,2-cyclohexanedione (CHD) and dipyridamole (DP) each inhibit the transport site 35Cl NMR line broadening, but neither competes with Cl- for binding. Thus these inhibitors do not occupy the transport site; instead they slow the migration of Cl- between the transport site and the medium. The simplest explanation for this behavior is that CHD and DP block one or more substrate channels. CHD is an arginine-specific covalent modification reagent, and its effectiveness as a channel blocker indicates that the channel contains arginine positive charges to facilitate the migration of anions through the channel. DP is a noncovalent channel blocker that binds with a stoichiometry of 1 molecule per band 3 dimer. DP binding is unaffected by CHD but is prevented by phenylglyoxal (PG), 4,4'-dinitrostilbene-2,2'-disulfonate (DNDS), or niflumic acid. Thus the DP and CHD binding sites are distinct, with DP binding sufficiently close to the transport site to interact with PG and DNDS. It is proposed that substrate channels may be a general feature of transport proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7895-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Molecular mechanisms of band 3 inhibitors. 2. Channel blockers.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.