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Structure paper

TitleThe mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures.
Journal, issue, pagesStructure, Vol. 32, Page 2337-2351.e4, Year 2024
Publish dateNov 4, 2021 (structure data deposition date)
AuthorsBradshaw, W.J. / Harris, G. / Gileadi, O. / Katis, V.L.
External linksStructure / PubMed:39442513
MethodsX-ray diffraction
Resolution1.9 - 2.4 Å
Structure data

PDB-7q5t:
The tandem SH2 domains of SYK with a bound FCER1G diphospho-ITAM peptide
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7q5u:
The tandem SH2 domains of SYK with a bound CD3G diphospho-ITAM peptide
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-7q5w:
The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7q63:
The tandem SH2 domains of SYK
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-P4G:
1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE

ChemComp-SCN:
THIOCYANATE ION

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Signalling / kinase

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