PDBsum entry 1nyg

Phosphotransferase

PDB id: 1nyg

Contents

Protein chain

58 a.a. *

* Residue conservation analysis

PDB id:

1nyg

Name:

Phosphotransferase

Title:

Nmr study of the sh3 domain from fyn proto-oncogene tyrosine kinase, family of 20 structures

Structure:

Fyn. Chain: a. Fragment: sh3 domain, residues 82 - 148. Engineered: yes. Mutation: yes. Other_details: n-terminal gs from expression system

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

C.J.Morton,D.J.R.Pugh,I.D.Campbell

Key ref:

C.J.Morton et al. (1996). Solution structure and peptide binding of the SH3 domain from human Fyn. Structure, 4, 705-714. PubMed id: 8805554 DOI: 10.1016/S0969-2126(96)00076-7

Date:

22-Apr-96 Release date: 08-Nov-96

Protein chain

P06241  (FYN_HUMAN) -  Tyrosine-protein kinase Fyn from Homo sapiens

Seq: 537 a.a.

Struc: 58 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.10.2 - non-specific protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/S0969-2126(96)00076-7

Structure 4:705-714 (1996)

PubMed id: 8805554

Solution structure and peptide binding of the SH3 domain from human Fyn.

C.J.Morton, D.J.Pugh, E.L.Brown, J.D.Kahmann, D.A.Renzoni, I.D.Campbell.

ABSTRACT

BACKGROUND: The Src family of tyrosine kinases is involved in the propagation of intracellular signals from many transmembrane receptors. Each member of the family contains two domains that regulate interactions with other molecules, one of which is the Src homology 3 (SH3) domain. Although structures have previously been determined for SH3 domains, and ideas about peptide-binding modes have been proposed, their physiological role is still unclear. RESULTS: We have determined the solution structure of the SH3 domain from the Src family tyrosine kinase Fyn in two forms: unbound and complexed with a peptide corresponding to a putative ligand sequence from phosphatidylinositol 3' kinase. Fyn SH3 shows the typical SH3 topology of two perpendicular three-stranded beta sheets and a single turn of 3(10) helix. The interaction of SH3 with three potential ligand peptides was investigated, demonstrating that they all bind to the same site on the molecule. A previous model for ligand binding to SH3 domains predicts binding in one of two orientations (class I or II), each characterized by a consensus sequence. The ligand with the closest match to the class I consensus sequence bound with highest affinity and in the predicted orientation. CONCLUSIONS: The Fyn SH3 domain has a well-defined structure in solution. The relative binding affinities of the three ligand peptides and their orientation within the Fyn SH3 complex were consistent with recently proposed models for the binding of 'consensus' polyproline sequences. Although the affinities of consensus and non-consensus peptides are different, the degree of difference is not very large, suggesting that SH3 domains bind to polyproline peptides in a promiscuous manner.

Selected figure(s)

Figure 3.
Figure 3. Diagrammatic representation of the Fyn SH3 structure, showing the position of the two β sheets and the single turn of 3[10] helix. Strands are coloured green in β sheet I and yellow in β sheet II, with the 3[10] helix coloured blue. The N and C termini are indicated. This figure was prepared with the programs MOLSCRIPT [45] and Raster3D [46 and 47]. Figure 3. Diagrammatic representation of the Fyn SH3 structure, showing the position of the two β sheets and the single turn of 3[10] helix. Strands are coloured green in β sheet I and yellow in β sheet II, with the 3[10] helix coloured blue. The N and C termini are indicated. This figure was prepared with the programs MOLSCRIPT [[3]45] and Raster3D [[4]46 and [5]47].

Figure 4.
Figure 4. The structure of the Fyn SH3–peptide 2 complex. The protein is shown as a backbone worm, with residues displaying NOE crosspeaks with the peptide shown as sticks. These are Tyr91 (red), Tyr137 (cyan), Asn136 (yellow) and Trp119 (green). The peptide is displayed as a ball and stick structure, coloured by atom type, with the N terminus on the right of the picture. Figure 4. The structure of the Fyn SH3–peptide 2 complex. The protein is shown as a backbone worm, with residues displaying NOE crosspeaks with the peptide shown as sticks. These are Tyr91 (red), Tyr137 (cyan), Asn136 (yellow) and Trp119 (green). The peptide is displayed as a ball and stick structure, coloured by atom type, with the N terminus on the right of the picture.

The above figures are reprinted by permission from Cell Press: Structure (1996, 4, 705-714) copyright 1996.

Figures were selected by an automated process.