Solution Structure of the Human Grb7-SH2 Domain/erbB2 Peptide Complex and Structural Basis for Grb7 Binding to ErbB2

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2003 Sep 17

PMID 12975581

Citations 16

Authors

Monika Ivancic

Roger J Daly

Barbara A Lyons

Affiliations

Soon will be listed here.

Abstract

The solution structure of the hGrb7-SH2 domain in complex with a ten amino acid phosphorylated peptide ligand representative of the erbB2 receptor tyrosine kinase (pY1139) is presented as determined by nuclear magnetic resonance methods. The hGrb7-SH2 domain structure reveals the Src homology 2 domain topology consisting of a central beta-sheet capped at each end by an alpha-helix. The presence of a four residue insertion in the region between beta-strand E and the EF loop and resulting influences on the SH2 domain/peptide complex structure are discussed. The binding conformation of the erbB2 peptide is in a beta-turn similar to that found in phosphorylated tyrosine peptides bound to the Grb2-SH2 domain. To our knowledge this is only the second example of an SH2 domain binding its naturally occurring ligands in a turn, instead of extended, conformation. Close contacts between residues responsible for binding specificity in hGrb7-SH2 and the erbB2 peptide are characterized and the potential effect of mutation of these residues on the hGrb7-SH2 domain structure is discussed.

Citing Articles

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Godamudunage M, Foster A, Warren D, Lyons B J Mol Recognit. 2017; 30(8).

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Preparation of crystals for characterizing the Grb7 SH2 domain before and after complex formation with a bicyclic peptide antagonist.

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Dimerization in the Grb7 protein.

Peterson T, Benallie R, Bradford A, Pias S, Yazzie J, Lor S J Mol Recognit. 2012; 25(8):427-34.

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Water-refined solution structure of the human Grb7-SH2 domain in complex with the erbB2 receptor peptide pY1139.

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