Exploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of Hsp70.

NUCLEOTIDE BINDING DOMAIN, UNP RESIDUES 1-380

HEAT SHOCK 70 KDA PROTEIN 1, HSP70-1, HSP70.1

GPLGSMAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIG
RKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQR
QATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDN
RLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLE
PVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILIKSTRAAAS

17-28% (W/V) PEG3350, 0.1 M HEPES PH 7.5, 2 MM MGCL2, 2 MM NAH2PO4 AND 5 MM INHIBITOR

FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL ROLE OF ATP-BINDING SITE RESIDUES

RESIDUES 382 ONWARDS ARE A CLONING ARTEFACT DERIVED FROM THE EXPRESSION VECTOR PGEX-6P-1

HEAT SHOCK PROTEIN, HSP70, HSP72, ATPASE, CHAPERONE, ADENOSINE, INHIBITOR