Literature DB >> 1834945

Peptide-binding specificity of the molecular chaperone BiP.

G C Flynn1, J Pohl, M T Flocco, J E Rothman.   

Abstract

Members of the heat-shock protein family (hsp70s) can distinguish folded from unfolded proteins. This property is crucial to the role of hsp70s as molecular chaperones and is attributable to the amino-acid specificity of the peptide-binding site. The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length. The peptide-binding site selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein.

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Year:  1991        PMID: 1834945     DOI: 10.1038/353726a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  205 in total

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Authors:  C M Story; M H Furman; H L Ploegh
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Authors:  R A Ivey; C Subramanian; B D Bruce
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Journal:  Biochem J       Date:  2001-03-15       Impact factor: 3.857

5.  Characterization and regulation of the major histocompatibility complex-encoded proteins Hsp70-Hom and Hsp70-1/2.

Authors:  A M Fourie; P A Peterson; Y Yang
Journal:  Cell Stress Chaperones       Date:  2001-07       Impact factor: 3.667

6.  High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer.

Authors:  Yoshinari Miyata; Lyra Chang; Anthony Bainor; Thomas J McQuade; Christopher P Walczak; Yaru Zhang; Martha J Larsen; Paul Kirchhoff; Jason E Gestwicki
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7.  A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.

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Authors:  Carissa L Young; David L Raden; Anne S Robinson
Journal:  Traffic       Date:  2013-02-04       Impact factor: 6.215

9.  Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR.

Authors:  P J Thomas; P L Pedersen
Journal:  J Bioenerg Biomembr       Date:  1993-02       Impact factor: 2.945

10.  SAHA enhances Proteostasis of epilepsy-associated α1(A322D)β2γ2 GABA(A) receptors.

Authors:  Xiao-Jing Di; Dong-Yun Han; Ya-Juan Wang; Mark R Chance; Ting-Wei Mu
Journal:  Chem Biol       Date:  2013-11-07
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