3UA6

Crystal Structure of the Human Fyn SH3 domain

Summary for 3UA6

• Entry DOI: 10.2210/pdb3ua6/pdb
• Related: 1SHF 3UA7
• Descriptor: Tyrosine-protein kinase Fyn, GLYCEROL, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: beta barrel, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P06241
• Total number of polymer chains: 2
• Total formula weight: 14872.84

Authors

Camara-Artigas, A.,Martin-Garcia, J.M. (deposition date: 2011-10-21, release date: 2012-07-25, Last modification date: 2023-09-13)

Primary citation

Martin-Garcia, J.M.,Luque, I.,Ruiz-Sanz, J.,Camara-Artigas, A.
The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein.
Acta Crystallogr.,Sect.D, 68:1030-1040, 2012

PubMed Abstract: The hepatitis C virus nonstructural 5A (NS5A) protein is a large zinc-binding phosphoprotein that plays an important role in viral RNA replication and is involved in altering signal transduction pathways in the host cell. This protein interacts with Fyn tyrosine kinase in vivo and regulates its kinase activity. The 1.5 Å resolution crystal structure of a complex between the SH3 domain of the Fyn tyrosine kinase and the C-terminal proline-rich motif of the NS5A-derived peptide APPIPPPRRKR has been solved. Crystals were obtained in the presence of ZnCl(2) and belonged to the tetragonal space group P4(1)2(1)2. The asymmetric unit is composed of four SH3 domains and two NS5A peptide molecules; only three of the domain molecules contain a bound peptide, while the fourth molecule seems to correspond to a free form of the domain. Additionally, two of the SH3 domains are bound to the same peptide chain and form a ternary complex. The proline-rich motif present in the NS5A protein seems to be important for RNA replication and virus assembly, and the promiscuous interaction of the Fyn SH3 domain with the NS5A C-terminal proline-rich peptide found in this crystallographic structure may be important in the virus infection cycle.

PubMed: 22868769
DOI: 10.1107/S0907444912019798

Experimental method

X-RAY DIFFRACTION (1.85 Å)