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2001 | 48 | 4 | 867-875

Article title

Structural basis of negative cooperativity in transthyretin

Content

Title variants

Languages of publication

EN

Abstracts

EN
A comparison of the AC and BD binding sites of transthyretin (TTR) was made in terms of the interatomic distances between the Cα atoms of equivalent amino acids, measured across the tetramer channel in each binding site. The comparison of the channel diameter for apo TTR from different sources revealed that in the unliganded transthyretin tetramers the distances between the A, D and H β-strands are consistently larger, while the distances between the G β-strands are smaller in one site than in the other. These differences might be described to have a 'wave' character. An analogous analysis performed for transthyretin complexes reveals that the shape of the plot is similar, although the amplitudes of the changes are smaller. The analysis leads us to a model of the changes in the binding sites caused by ligand binding. The sequence of events includes ligand binding in the first site, followed by a slight collapse of this site and concomitant opening of the second site, binding of the second molecule and collapse of the second site. The following opening of the first, already occupied site upon ligand binding in the second site is smaller because of the bridging interactions already formed by the first ligand. This explains the negative cooperativity (NC) effect observed for many ligands in transthyretin.

Year

Volume

48

Issue

4

Pages

867-875

Physical description

Dates

published
2001
received
2001-10-16
accepted
2001-12-3

Contributors

author
  • Institute of Chemistry, Nicolaus Copernicus University, Toruń, Poland
author
  • Hauptman-Woodward Medical Research Institute, Inc., Buffalo, U.S.A.
  • Institute of Chemistry, Nicolaus Copernicus University, Toruń, Poland

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv48i4p867kz
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