PDBsum entry 5hck

Transferase

PDB id: 5hck

Contents

Protein chain

61 a.a. *

* Residue conservation analysis

PDB id:

5hck

Name:

Transferase

Title:

Human hck sh3 domain, nmr, minimized average structure

Structure:

Hematopoietic cell kinase. Chain: a. Fragment: sh3 domain. Synonym: hck. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Gene: residues g72-e143 of human hck. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

D.A.Horita,D.M.Baldisseri,W.Zhang,A.S.Altieri,T.E.Smithgall, W.H.Gmeiner,R.A.Byrd

Key ref:

D.A.Horita et al. (1998). Solution structure of the human Hck SH3 domain and identification of its ligand binding site. J Mol Biol, 278, 253-265. PubMed id: 9571048 DOI: 10.1006/jmbi.1998.1690

Date:

09-Mar-98 Release date: 17-Jun-98

Protein chain

P08631  (HCK_HUMAN) -  Tyrosine-protein kinase HCK from Homo sapiens

Seq: 526 a.a.

Struc: 61 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: 10.1006/jmbi.1998.1690

J Mol Biol 278:253-265 (1998)

PubMed id: 9571048

Solution structure of the human Hck SH3 domain and identification of its ligand binding site.

D.A.Horita, D.M.Baldisseri, W.Zhang, A.S.Altieri, T.E.Smithgall, W.H.Gmeiner, R.A.Byrd.

ABSTRACT

SH3 domains are protein binding domains that occur widely among signal transduction proteins. Here, we present the NMR-determined solution structure of the SH3 domain from the cytoplasmic protein tyrosine kinase, Hck. Hck is involved in a number of cell signal transduction pathways, frequently in pathways associated with immune response. SH3 domains bind proteins via a left-handed polyproline type II helix on the target protein. We have assessed the structural impact of binding to a ligand through addition of a peptide corresponding to a proline-rich region of a Hck target, the GTPase activating protein of the Ras pathway. Ligand binding effects small structural changes and stabilizes the SH3 domain structure. Also, we have compared the solution structure of the Hck SH3 domain to the crystal structure of Hck, in which the SH3 domain exhibits an intramolecular binding to an interdomain linker region. These structures are interpreted as the apo- and holo- forms of the Hck SH3 domain.

Selected figure(s)

Figure 1.
Figure 1. Domain structure of human p60^hckand sequence and secondary structural alignment for the Hck SH3 domain. Residues listed in italics were excluded from the structure calculation. Numbering for p59^hckstarts at p60^hckresidue 21.

Figure 9.
Figure 9. Superimposition of residues W114 and I128 to V133 of the minimized average NMR structure (blue) with the corresponding residues for the SH3 domain (red) and the PXXP motif (green) from the Hck crystal structure (PDB entry 1ad5). Superimposition of the SH3 domains was calculated to minimize the RMSD for strands ba, bb, bc, and be.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1998, 278, 253-265) copyright 1998.

Figures were selected by an automated process.