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1NYF

NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE

Summary for 1NYF
Entry DOI10.2210/pdb1nyf/pdb
DescriptorFYN (1 entity in total)
Functional Keywordssh3 domain, polyproline-binding, phosphotransferase
Biological sourceHomo sapiens (human)
Cellular locationCell membrane: P06241
Total number of polymer chains1
Total formula weight7554.11
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 citationMorton, 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: 8805554
DOI: 10.1016/S0969-2126(96)00076-7
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-11-06公开中

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