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Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain.

The Journal of biological chemistry - 5 Apr 1993

Gaut J R, Hendershot L M

Abstract excerpt

Immunoglobulin-binding protein (BiP), a 70-kDa heat shock protein in the endoplasmic reticulum, binds transiently to nascent proteins, releasing them upon folding and assembly. The in vitro release of bound proteins from BiP requires ATP hydrolysis. Recently, the three-dimensional structure was solved for an ATP-hydrolyzing proteolytic 44-kDa fragment of a 71-kDa heat shock cognate protein, HSC71. Because of the...

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PMID: 8463260

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Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain.PMID 8463260Read ↗

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Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.Semantic proximity Read ↗

An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein.Semantic proximity Read ↗

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