PDBsum entry 1mw4

Hormone/growth factor/transferase

PDB id: 1mw4

Contents

Protein chain

120 a.a. *

Ligands

PRO-GLN-PRO-GLU-PTR-VAL-ASN-GLN-PRO-ASP

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: Solution structure of the human grb7-Sh2 domain/erbb2 peptide complex and structural basis for grb7 binding to erbb2.
• Authors: M.Ivancic, R.J.Daly, B.A.Lyons.
• Ref.: J Biomol Nmr, 2003, 27, 205-219.
• PubMed id: 12975581

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.

Secondary reference #1

• Title: Assignment of backbone 1h, 13c, And 15n resonances of human grb7-Sh2 domain in complex with a phosphorylated peptide ligand.
• Authors: P.J.Brescia, M.Ivancic, B.A.Lyons.
• Ref.: J Biomol Nmr, 2002, 23, 77-78.
• PubMed id: 12061724