An Intramolecular Switch Regulates Phosphoindependent FHA Domain Interactions in Mycobacterium tuberculosis-Reference-Cited by-同舟云学术

An Intramolecular Switch Regulates Phosphoindependent FHA Domain Interactions in Mycobacterium tuberculosis

Published:2009-03-24 Issue:63 Volume:2 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Nott Timothy J.¹,Kelly Geoff²,Stach Lasse¹,Li Jiejin¹,Westcott Sarah¹,Patel Dony¹,Hunt Debbie M.³,Howell Steven¹,Buxton Roger S.³,O’Hare Helen M.⁴⁵,Smerdon Stephen J.¹

Affiliation:

1. Division of Molecular Structure, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.

2. Biomedical NMR Centre, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.

3. Division of Mycobacterial Research, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.

4. Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, UK.

5. Department of Biochemistry, University of Leicester, Leicester LE1 9HN, UK.

Abstract

Binding of Rv1827 to target proteins through its forkhead-associated (FHA) domain does not require their prior phosphorylation at threonine residues.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. The Protein Kinase Complement of the Human Genome

2. Reading protein modifications with interaction domains

3. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors

4. The FHA Domain Is a Modular Phosphopeptide Recognition Motif

5. The Molecular Basis of FHA Domain:Phosphopeptide Binding Specificity and Implications for Phospho-Dependent Signaling Mechanisms

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