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. 2009 Oct 23;5(10):e1000541. doi: 10.1371/journal.pcbi.1000541

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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A Subset of the sequence similarity network from Fig. 4, with nodes colored according to the identity of the amino acid predicted to occcupy the position of the cis-proline at the N-terminus of beta strand 3 in the Trx fold (Pro 75 in human Trx 1). The orange path traces transitive sequence similarity relationships between human Trx 2, passing through B. japonicum CMP (CYCY_BRAJA), and ending at bovine Prx 3 (PRDX3_BOVIN). Large nodes represent sequences that are associated with the structures from Fig. 3. Predictions are based on sequence alignments to PFAM Thioredoxin-like Clan HMMs. B The same path—connecting the structures associated with the sequences in A—traced through a subset of the structure-based network from Fig. 3B. C The same path traced through a subset of the structure-based hierarchical clustering of representative structures from Fig. 3D.