4HCK

HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES

4HCK の概要

• エントリーDOI: 10.2210/pdb4hck/pdb
• 分子名称: HEMATOPOIETIC CELL KINASE (1 entity in total)
• 機能のキーワード: sh3, protein tyrosine kinase, signal transduction, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Lysosome. Isoform 2: Cell membrane; Lipid-anchor. Cytoplasmic vesicle, secretory vesicle: P08631
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8240.03

構造登録者

Horita, D.A.,Baldisseri, D.M.,Zhang, W.,Altieri, A.S.,Smithgall, T.E.,Gmeiner, W.H.,Byrd, R.A. (登録日: 1998-03-09, 公開日: 1998-06-17, 最終更新日: 2024-05-01)

主引用文献

Horita, D.A.,Baldisseri, D.M.,Zhang, W.,Altieri, A.S.,Smithgall, T.E.,Gmeiner, W.H.,Byrd, R.A.
Solution structure of the human Hck SH3 domain and identification of its ligand binding site.
J.Mol.Biol., 278:253-265, 1998

PubMed 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.

PubMed: 9571048
DOI: 10.1006/jmbi.1998.1690

実験手法

SOLUTION NMR