2HDA

Yes SH3 domain

Summary for 2HDA

• Entry DOI: 10.2210/pdb2hda/pdb
• Descriptor: Proto-oncogene tyrosine-protein kinase Yes, SULFATE ION (3 entities in total)
• Functional Keywords: main beta, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane: P07947
• Total number of polymer chains: 1
• Total formula weight: 7224.88

Authors

Camara-Artigas, A.,Luque, I.,Ruiz-Sanz, J.,Mateo, P.L.,Martin-Garcia, J.M. (deposition date: 2006-06-20, release date: 2007-04-17, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)