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Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers.

ABSTRACT: The formation of homodimer complexes for interface stability, catalysis and regulation is intriguing. The mechanisms of homodimer complexations are even more interesting. Some homodimers form without intermediates (two-state (2S)) and others through the formation of stable intermediates (three-state (3S)). Here, we analyze 41 homodimer (25 2S and 16 3S) structures determined by X-ray crystallography to estimate structural differences between them. The analysis suggests that a combination of structural properties such as monomer length, subunit interface area, ratio of interface to interior hydrophobicity can predominately distinguish 2S and 3S homodimers. These findings are useful in the prediction of homodimer folding and binding mechanisms using structural data.

SUBMITTER: Li L

PROVIDER: S-EPMC1891634 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature

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Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers.

Li Lei L Gunasekaran Kannan K Gan Jacob Gah-Kok JG Zhanhua Cui C Shapshak Paul P Sakharkar Meena Kishore MK Kangueane Pandjassarame P

Bioinformation 20050902 2

The formation of homodimer complexes for interface stability, catalysis and regulation is intriguing. The mechanisms of homodimer complexations are even more interesting. Some homodimers form without intermediates (two-state (2S)) and others through the formation of stable intermediates (three-state (3S)). Here, we analyze 41 homodimer (25 2S and 16 3S) structures determined by X-ray crystallography to estimate structural differences between them. The analysis suggests that a combination of stru ...[more]

PMID: 17597851

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