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Comment
. 2010 Dec 8;18(12):1549-50.
doi: 10.1016/j.str.2010.11.005.

FHA domain pThr binding specificity: it's all about me

Nicolas Coquelle  1 , J N Mark Glover
Affiliations
Comment

FHA domain pThr binding specificity: it's all about me

Nicolas Coquelle et al. Structure. .

Abstract

The FHA domain is a phospho-peptide binding module involved in a wide range of cellular pathways, with a striking specificity for phospho-threonine over phospho-serine binding partners. Biochemical, structural, and dynamic simulations analysis allowed Pennell and colleagues to unravel the molecular basis of FHA domain phospho-threonine specificity.

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Figures

Figure 1
Figure 1. Structure of the Rad53p FHA Bound to a Cognate pThr-Containing Peptide
(A) Overview of the Rad53p FHA phospho-peptide complex. (B) Detailed view of FHA phospho-peptide interactions, highlighting key residues that contact the pThr and downstream residues in the phospho-peptide target.
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Comment on

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