Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study.
The 90 kDa heat shock protein (hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins including steroid receptors. Here we provide the first numerical analysis of hsp90-target associations using surface plasmon resonance. Binding affinities of histones, the "native molten globule", casein and calmodulin to hsp90 decrease in the order of Kd = 70 +/- 24, 220 +/- 70 and 1800 +/- 600 nM, respectively. Analysis of the structure of binding proteins revealed that their binding affinity depends on both hydrophobicity and positive charges making the discriminative features of hsp90 similar to those of other molecular chaperones.
Csermely
P
P
Department of Medical Chemistry, Semmelweis University, School of Medicine, Budapest, Hungary. csermely@puskin.sote.hu
Miyata
Y
Y
Söti
C
C
Yahara
I
I
D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D015374:Biosensing Techniques; D002147:Calmodulin / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D011485:Protein Binding; D013499:Surface Properties
D002147:Calmodulin; D002364:Caseins; D018841:HSP90 Heat-Shock Proteins; D006657:Histones; D000255:Adenosine Triphosphate