2HDA

Yes SH3 domain

2HDA の概要

• エントリーDOI: 10.2210/pdb2hda/pdb
• 分子名称: Proto-oncogene tyrosine-protein kinase Yes, SULFATE ION (3 entities in total)
• 機能のキーワード: main beta, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane: P07947
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7224.88

構造登録者

Camara-Artigas, A.,Luque, I.,Ruiz-Sanz, J.,Mateo, P.L.,Martin-Garcia, J.M. (登録日: 2006-06-20, 公開日: 2007-04-17, 最終更新日: 2023-08-30)

主引用文献

Martin-Garcia, J.M.,Luque, I.,Mateo, P.L.,Ruiz-Sanz, J.,Camara-Artigas, A.
Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation.
Febs Lett., 581:1701-1706, 2007

PubMed Abstract: SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family.

PubMed: 17418139
DOI: 10.1016/j.febslet.2007.03.059

実験手法

X-RAY DIFFRACTION (1.9 Å)