1AOT

NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, MINIMIZED AVERAGE STRUCTURE

Summary for 1AOT

• Entry DOI: 10.2210/pdb1aot/pdb
• Related: 1AOU
• Descriptor: FYN PROTEIN-TYROSINE KINASE, PHOSPHOTYROSYL PEPTIDE (2 entities in total)
• Functional Keywords: sh2 domain, signal transduction, peptide complex, complex (proto-oncogene-early protein), complex (proto-oncogene-early protein) complex, complex (proto-oncogene/early protein)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane: P06241; Host membrane; Single-pass membrane protein (Potential): P03079
• Total number of polymer chains: 2
• Total formula weight: 13773.33

Authors

Mulhern, T.D.,Shaw, G.L.,Morton, C.J.,Day, A.J.,Campbell, I.D. (deposition date: 1997-07-10, release date: 1998-01-14, Last modification date: 2024-10-23)

Primary citation

Mulhern, T.D.,Shaw, G.L.,Morton, C.J.,Day, A.J.,Campbell, I.D.
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
Structure, 5:1313-1323, 1997

PubMed Abstract: SH2 domains are found in a variety of signal transduction proteins; they bind phosphotyrosine-containing sequences, allowing them to both recognize target molecules and regulate intramolecular kinase activity. Fyn is a member of the Src family of tyrosine kinases that are involved in signal transduction by association with a number of membrane receptors. The kinase activity of these signalling proteins is modulated by switching the binding mode of their SH2 and SH3 domains from intramolecular to intermolecular. The molecular basis of the signalling roles observed for different Src family members is still not well understood; although structures have been determined for the SH2 domains of other Src family molecules, this is the first structure of the Fyn SH2 domain.

PubMed: 9351806
DOI: 10.1016/S0969-2126(97)00283-9

Experimental method

SOLUTION NMR