1NYF
NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE
Summary for 1NYF
Entry DOI | 10.2210/pdb1nyf/pdb |
Descriptor | FYN (1 entity in total) |
Functional Keywords | sh3 domain, polyproline-binding, phosphotransferase |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane: P06241 |
Total number of polymer chains | 1 |
Total formula weight | 7554.11 |
Authors | Morton, C.J.,Pugh, D.J.R.,Campbell, I.D. (deposition date: 1996-04-22, release date: 1996-11-08, Last modification date: 2024-05-22) |
Primary citation | Morton, C.J.,Pugh, D.J.,Brown, E.L.,Kahmann, J.D.,Renzoni, D.A.,Campbell, I.D. Solution structure and peptide binding of the SH3 domain from human Fyn. Structure, 4:705-714, 1996 Cited by PubMed Abstract: The Src family of tyrosine kinases is involved in the propagation of intracellular signals from many transmembrane receptors. Each member of the family contains two domains that regulate interactions with other molecules, one of which is the Src homology 3 (SH3) domain. Although structures have previously been determined for SH3 domains, and ideas about peptide-binding modes have been proposed, their physiological role is still unclear. PubMed: 8805554DOI: 10.1016/S0969-2126(96)00076-7 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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