PDBsum entry 3u3f

Transferase/signaling protein

PDB id: 3u3f

Contents

Protein chains

130 a.a.

13 a.a.

12 a.a.

14 a.a.

Ligands

GLU-LEU-ASP-GLU-LEU-MET-ALA-SER-LEU-SER ×2

Waters ×3

PDB id:

3u3f

Name:

Transferase/signaling protein

Title:

Structural basis for the interaction of pyk2 pat domain with paxillin ld motifs

Structure:

Protein-tyrosine kinase 2-beta. Chain: a, b, c, d. Fragment: unp residues 871-1005. Synonym: focal adhesion kinase 2, fadk 2, raftk. Engineered: yes. Mutation: yes. Paxillin ld2 peptide. Chain: e, f, g, h, i, j. Fragment: unp residues 261-277.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ptk2b, fak2, pyk2, raftk. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: synthetic peptide

Resolution:

3.10Å R-factor: 0.220 R-free: 0.266

Authors:

M.Vanarotti,D.J.Miller,C.C.Guibao,J.J.Zheng

Key ref:

M.S.Vanarotti et al. (2014). Structural and mechanistic insights into the interaction between Pyk2 and paxillin LD motifs. J Mol Biol, 426, 3985-4001. PubMed id: 25174335 DOI: 10.1016/j.jmb.2014.08.014

Date:

05-Oct-11 Release date: 24-Oct-12

Protein chains

Q14289  (FAK2_HUMAN) -  Protein-tyrosine kinase 2-beta from Homo sapiens

Seq: 1009 a.a.

Struc: 130 a.a.*

Protein chains

P49023  (PAXI_HUMAN) -  Paxillin from Homo sapiens

Seq: 591 a.a.

Struc: 13 a.a.

Protein chain

P49023  (PAXI_HUMAN) -  Paxillin from Homo sapiens

Seq: 591 a.a.

Struc: 12 a.a.

Protein chain

P49023  (PAXI_HUMAN) -  Paxillin from Homo sapiens

Seq: 591 a.a.

Struc: 14 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: 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/j.jmb.2014.08.014

J Mol Biol 426:3985-4001 (2014)

PubMed id: 25174335

Structural and mechanistic insights into the interaction between Pyk2 and paxillin LD motifs.

M.S.Vanarotti, D.J.Miller, C.D.Guibao, A.Nourse, J.J.Zheng.

ABSTRACT

Proline-rich tyrosine kinase 2 (Pyk2) is a member of the focal adhesion kinase (FAK) subfamily of cytoplasmic tyrosine kinases. The C-terminal Pyk2-focal adhesion targeting (FAT) domain binds to paxillin, an adhesion molecule. Paxillin has five leucine-aspartate (LD) motifs (LD1-LD5). Here, we show that the second LD motif of paxillin, LD2, interacts with Pyk2-FAT, similar to the known Pyk2-FAT/LD4 interaction. Both LD motifs can target two ligand binding sites on Pyk2-FAT. Interestingly, they also share similar binding affinity for Pyk2-FAT with preferential association to one site relative to the other. Nevertheless, the LD2-LD4 region of paxillin (paxillin(133-290)) binds to Pyk2-FAT as a 1:1 complex. However, our data suggest that the Pyk2-FAT and paxillin complex is dynamic and it appears to be a mixture of two distinct conformations of paxillin that almost equally compete for Pyk2-FAT binding. These studies provide insight into the underlying selectivity of paxillin for Pyk2 and FAK that may influence the differing behavior of these two closely related kinases in focal adhesion sites.