Linked Life Data

16204882

Source:http://linkedlifedata.com/resource/pubmed/id/16204882

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 10
pubmed:dateCreated
2005-10-5
pubmed:abstractText
The crystal structure of the complex of human transthyretin (hTTR) with 3,3',5,5'-tetraiodothyroacetic acid (T4Ac) has been determined to 2.2 Angstrom resolution. The complex crystallizes in the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 43.46, b = 85.85, c = 65.44 Angstrom. The structure was refined to R = 17.3% and R(free) = 21.9% for reflections without any sigma-cutoff. T4Ac is bound in both the forward and the reverse mode in the two binding sites of hTTR. In the forward orientation, T4Ac binds in a position similar to that described for thyroxine (T4) in the orthorhombic hTTR-T4 complex. In this orientation, the iodine substituents of the phenolic ring are bound in the P3'/P2 halogen pockets. In the reverse orientation, which is the major binding mode of T4Ac, the ligand is bound deep in the TTR channel, with the carboxylic group bound in the P3' pocket and forming simultaneous polar interactions with the residues constituting the two hormone-binding sites. Such interactions of a thyroxine-analogue ligand bound in the reverse mode have never been observed in TTR complexes previously.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1313-9
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Ligand binding at the transthyretin dimer-dimer interface: structure of the transthyretin-T4Ac complex at 2.2 Angstrom resolution.
pubmed:affiliation
Institute of Chemistry, N. Copernicus University, Gagarina 7, 87-100 Toru?, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't