2021年1月3日 · 7BFI A double-histidine mutant of HSP47 slows down client release at low pH. PDB DOI: https://doi.org/10.2210/pdb7BFI/pdb; Classification: CHAPERONE; Organism(s): Canis lupus familiaris, Homo sapiens; Expression System: Escherichia coli BL21(DE3) Mutation(s): Yes ; Deposited: 2021-01-03 Released: 2021-11-10 ; Deposition Author(s): Oecal, S ...

2021年12月1日 · Here, we employed a collagen II peptide library to characterize high-affinity binding sites for HSP47. We show that many previously predicted binding sites have very low affinities due to the presence of a negatively charged amino acid in the binding motif.

7BFI: A double-histidine mutant of HSP47 slows down client release at low pH

Biological Unit for 7BFI: pentameric; determined by author and by software (PISA)

2021年11月10日 · A double-histidine mutant of HSP47 slows down client release at low pH

Summary for 7BFI. Entry DOI: 10.2210/pdb7bfi/pdb: Related: 3ZHA 4AU2 4AU3 4AU4: Descriptor: Collagen-binding protein, 15R8 collagen model peptide (3 entities in total) Functional Keywords: hsp47, collagen-binding, ph-mediated client release, chaperone: Biological source: Canis lupus familiaris (Dog) More:

PDB Entry - 7BFI (Status - Released) Summary information: Title: A double-histidine mutant of HSP47 slows down client release at low pH. PDB DOI: https://doi.org/10.2210/pdb7bfi/pdb. Primary publication DOI: https://doi.org/10.1016/j.jbc.2021.101169. Entry authors: Oecal, S., Baumann, U. Initial deposition on: 3 January 2021

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

3D Structure of chain 7BFI_A - A DOUBLE-HISTIDINE MUTANT OF HSP47 SLOWS DOWN CLIENT RELEASE AT LOW PH - 7BFI | canSAR.ai

HSP47 is known to bind to the collagen triple-helix but the exact positions and numbers of binding sites are not clear. Here, we employed a collagen II peptide library to characterize high-affinity...