Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (Hsp). The 90 kDa Hsp90 is found in bacteria and eukaryotes. It is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation [1]. Hsp90 contains four domains and forms homodimers where the contact sites are localized within the C-terminus in the open conformation of the dimer, while the N-termini come into contact only in the closed conformation.
Asp f 12 is an IgE-binding Hsp90 from the mould Aspergillus fumigatus [2].
Family-defining Pfam domains (at least one of these domains is present in each family member):
| Pfam domain | Pfam clan | ||
| PF00183 | Hsp90 protein | - | |
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