2014年5月19日 · 4PLQ Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure. PDB DOI: https://doi.org/10.2210/pdb4PLQ/pdb; Classification: PEPTIDE BINDING PROTEIN; Organism(s): synthetic construct; Expression System: Escherichia coli; Mutation(s): No

2014年8月27日 · Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure. Changes made to a PDB entry after its initial release are considered to be either “major” or “minor”. The latest minor version of each major version is available as a file download.

4PLQ: Crystal Structures Of Designed Armadillo Repeat Proteins: Implications Of Construct Design And Crystallization Conditions On Overall Structure

2017年3月3日 · In this review, we discuss the methods developed for designing repeat proteins, the proteins designed and the new directions ahead. The repeated modularity implies that there is a continuum of structural features from section to section so that each unit can attach to a preceding one while providing the same interactions for a subsequent unit.

Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.

4plq is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Designed armadillo repeat proteins (dArmRP) are promising modular proteins for the engineering of binding molecules that recognize extended polypeptide chains.

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PDB Entry - 4PLQ (Status - Released) Summary information: Title: Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure. PDB DOI: https://doi.org/10.2210/pdb4plq/pdb. Primary publication DOI: https://doi.org/10.1002/pro.2535

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