Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.

Coto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC
Int J Biol Macromol 118(Pt A):693-706 (2018 Oct 15)
PMID: 29959008
doi: 10.1016/j.ijbiomac.2018.06.123 		Submitted to SASBDB: 2017 Jun 17
Published in SASBDB:

SASDC75 – Leishmania braziliensis SGT co-chaperone

SGT protein experimental SAS data
DAMFILT model
Sample: SGT protein dimer, 92 kDa Leishmania braziliensis protein
Buffer: 20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 May 14
RgGuinier 4.5 nm
Dmax 17.0 nm