Structural basis of negative cooperativity in transthyretin

• Autorzy: Neumann P. , Cody V. , Wojtczak A.
• Języki publikacji: EN

Abstrakty

EN

A comparison of the AC and BD binding sites of transthyretin (TTR) was made in terms of the interatomic distances between the Ca 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.

Słowa kluczowe

EN

negative cooperativity; serum; man; transthyretin; protein; amyloidosis; thyroxine

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2001
• Tom: 48
• Numer: 4
• Opis fizyczny: p.867-875,fig.

Twórcy

autor

Neumann P.

• Nicolaus Copernicus University, Gagarina 7, 87-100 Torun, Poland

autor

Cody V.

autor

Wojtczak A.

Bibliografia

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