PDBsum entry 4hvw

Signaling protein/peptide

PDB id: 4hvw

Contents

Protein chains

61 a.a.

13 a.a.

Ligands

ACE

SO4

Waters ×81

PDB id:

4hvw

Name:

Signaling protein/peptide

Title:

Crystal structure of the t98E C-src-sh3 domain mutant in complex with the high affinity peptide vsl12

Structure:

Proto-oncogene tyrosine-protein kinase src. Chain: a. Fragment: sh3 domain. Synonym: proto-oncogenE C-src, pp60c-src, p60-src. Engineered: yes. Mutation: yes. Synthetic peptide acetyl-vslarrplpplp. Chain: b. Engineered: yes

Source:

Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Gene: src. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: high affinity peptide designed from phage display experiments

Resolution:

0.98Å R-factor: 0.134 R-free: 0.141

Authors:

A.Camara-Artigas

Key ref:

J.Bacarizo and A.Camara-Artigas (2013). Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II. Acta Crystallogr D Biol Crystallogr, 69, 756-766. PubMed id: 23633584 DOI: 10.1107/S0907444913001522

Date:

07-Nov-12 Release date: 01-May-13

Protein chain

P00523  (SRC_CHICK) -  Proto-oncogene tyrosine-protein kinase Src from Gallus gallus

Seq: 533 a.a.

Struc: 61 a.a.*

Protein chain

No UniProt id for this chain

Struc: 12 a.a.

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: 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: 10.1107/S0907444913001522

Acta Crystallogr D Biol Crystallogr 69:756-766 (2013)

PubMed id: 23633584

Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II.

J.Bacarizo, A.Camara-Artigas.

ABSTRACT

The atomic resolution crystal structures of complexes between the SH3 domain of the c-Src tyrosine kinase and two high-affinity peptides belonging to class I and class II have been solved. The crystals of the Thr98Asp and Thr98Glu mutants in complex with the APP12 peptide (APPLPPRNRPRL) belonged to the trigonal space group P3121 and in both cases the asymmetric unit was composed of one molecule of the SH3-APP12 complex. The crystals of the Thr98Glu mutant in complex with the VSL12 peptide (VSLARRPLPLP) belonged to the trigonal space group P3221 and the asymmetric unit was also composed of a single molecule of the SH3-VSL12 complex. All crystals were obtained in the presence of PEG 300 under the same conditions as reported for the intertwined dimeric structure of the c-Src SH3 domain, but the presence of the peptide stabilizes the monomeric form of the domain. These structures allow a detailed analysis of the role of salt bridges, cation-π interactions and hydrogen bonds in the binding of proline-rich motifs to the c-Src SH3 domain. Moreover, these crystallographic structures allow the role of water molecules in the binding of these motifs to the c-Src SH3 domain to be studied for the first time.