Abstract
As part of structural investigations of components of the molecular motor, dynein, we prepared the light chain, Robl1_mouse, with and without an N-terminal His-tag. We found that the His-tag introduced a spurious binding site for a second protein, IC74. We propose a molecular mechanism for functional interference by the His-tag.
Keywords: Affinity tag, docking, dynein, NMR spectroscopy, protein dynamics, protein-protein interactions
Protein & Peptide Letters
Title: Cautionary Tail: The Presence of an N-Terminal Tag on Dynein Light-Chain Roadblock/LC7 Affects Its Interaction with a Functional Partner
Volume: 14 Issue: 3
Author(s): Jikui Song, John L. Markley, Jikui Song and John L. Markley
Affiliation:
Keywords: Affinity tag, docking, dynein, NMR spectroscopy, protein dynamics, protein-protein interactions
Abstract: As part of structural investigations of components of the molecular motor, dynein, we prepared the light chain, Robl1_mouse, with and without an N-terminal His-tag. We found that the His-tag introduced a spurious binding site for a second protein, IC74. We propose a molecular mechanism for functional interference by the His-tag.
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Cite this article as:
Song Jikui, Markley L. John, Jikui Song and John L. Markley , Cautionary Tail: The Presence of an N-Terminal Tag on Dynein Light-Chain Roadblock/LC7 Affects Its Interaction with a Functional Partner, Protein & Peptide Letters 2007; 14 (3) . https://dx.doi.org/10.2174/092986607780090801
DOI https://dx.doi.org/10.2174/092986607780090801 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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