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Disruption of the Productive Encounter Complex Results in Dysregulation of DIAPH1 Activity

ABSTRACT: Formins are characterized by a N-terminal regulatory domain, which binds to the C-terminal auto-inhibitory domain, yielding an inactive complex. Cross-Linking and tandem MS was used to characterized the disordered "RRKR" motif of the C-terminus, which is notably absent from solved crystallographic structures. These results were used with NMR spectroscopy to locate and understand the dynamics of this disordered region. The proteins were synthesized using recombinant techniques and purified using chromatographic techniques. Proteins were mixed in equi-molar concentrations with excess concentration of cross-linkers. Samples were analyzed using SDS-PAGE gels, excised for chemical processing, and subjected to Trypsin digestion. Resulting peptides were extracted using formic acid and acetonitrile, lyophilized, and stored until MS analysis

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Alexander Shekhtman

PROVIDER: PXD042130 | JPOST Repository | Thu May 11 00:00:00 BST 2023

REPOSITORIES: jPOST

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			Action	DRS
	AS20200123S1-DSG.raw	Raw
	AS20200226S1-BS3.raw	Raw
	AS20200226S2-BS(PEG)5.raw	Raw
	DID-DAD-BS3-S2.raw	Raw
	DID_DAD.Fasta	Fasta

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