Abstract: The presently disclosed subject matter discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Abstract: A recombinant stress response polypeptide that lacks an antigen binding domain, and methods for using the recombinant stress response polypeptide to elicit an immune response, for example an anti-tumor response, in a subject.

Abstract: An isolated GRP94 ligand binding domain polypeptide, a three-dimensional crystal structure of the same, and methods of using the same to design modulators of Hsp90 proteins.

Abstract: An isolated GRP94 ligand binding domain polypeptide, a three-dimensional crystal structure of the same, and methods of using the same to design modulators of Hsp90 proteins.

Abstract: An isolated GRP94 ligand binding domain polypeptide, a three-dimensional crystal structure of the same, and methods of using the same to design modulators of Hsp90 proteins.

Abstract: The presently disclosed subject matter discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Abstract: The present invention discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Abstract: An isolated GRP94 ligand binding domain polypeptide.

Abstract: We claim an isolated nucleic acid molecule encoding a ligand binding domain of glucose regulated protein of 94 kDa (GRP94), a chimeric polynucleotide consisting of said nucleic acid molecule operably linked to a heterologous promoter wherein said nucleic acid molecule is optionally linked to a polynucleotide encoding a heterologous polypeptide so as to form a fusion protein between the GRP94 ligand binding domain polypeptide and said heterologous polypeptide, a vector consisting of said chimeric polynucleotide, and a host cell comprising said chimeric polynucleotide.

Abstract: An isolated GRP94 ligand binding domain polypeptide, a three-dimensional crystal structure of the same, and methods of using the same to design modulators of Hsp90 proteins.

Abstract: A recombinant stress response polypeptide that lacks an antigen binding domain, and methods for using the recombinant stress response polypeptide to elicit an immune response, for example an anti-tumor response, in a subject.

Abstract: The present invention discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Abstract: An isolated GRP94 ligand binding domain polypeptide, an isolated polynucleotide encoding the same, and methods of using the same to identify modulators of Hsp90 proteins.

Abstract: A method of eliciting an immune response in a vertebrate subject. The method includes the administration to a vertebrate subject of a composition including an amount of a purified complex including calreticulin bound to an antigenic molecule to elicit an immune response to the antigenic molecule in the vertebrate subject. Therapeutic methods, compositions and kits are also disclosed wherein the elicited immune response is utilized as a treatment for cancer and for infectious diseases.