Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture.

Literature DB >> 22153508

The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture.

Andrew J Baldwin¹, Hadi Lioe, Gillian R Hilton, Lindsay A Baker, John L Rubinstein, Lewis E Kay, Justin L P Benesch.

Abstract

We report structural models for the most abundant oligomers populated by the polydisperse molecular chaperone αB-crystallin. Subunit connectivity is determined by using restraints obtained from nuclear magnetic resonance spectroscopy and mass spectrometry measurements, enabling the construction of various oligomeric models. These candidate structures are filtered according to their correspondence with ion-mobility spectrometry data and cross-validated by using electron microscopy. The ensuing best-fit structures reveal the polyhedral architecture of αB-crystallin oligomers, and provide a rationale for their polydispersity and facile interconversion.

Entities: Chemical Gene

Mesh：

Substances：
alpha-Crystallin B Chain

Year: 2011 PMID： 22153508 DOI： 10.1016/j.str.2011.09.015

Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006

Keyword Cloud
Cited

40 in total

Review 1. Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.

Authors: Erin Thornell; Andrew Aquilina
Journal: Cell Mol Life Sci Date: 2015-07-26 Impact factor: 9.261

2. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.

Authors: Andi Mainz; Jirka Peschek; Maria Stavropoulou; Katrin C Back; Benjamin Bardiaux; Sam Asami; Elke Prade; Carsten Peters; Sevil Weinkauf; Johannes Buchner; Bernd Reif
Journal: Nat Struct Mol Biol Date: 2015-10-12 Impact factor: 15.369

3. Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.

Authors: Kenneth J Laszlo; Matthew F Bush
Journal: Anal Chem Date: 2017-07-07 Impact factor: 6.986

4. The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.

Authors: John A Carver; Aidan B Grosas; Heath Ecroyd; Roy A Quinlan
Journal: Cell Stress Chaperones Date: 2017-04-08 Impact factor: 3.667

5. Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.

Authors: Michelle Heirbaut; Frederik Lermyte; Esther M Martin; Steven Beelen; Frank Sobott; Sergei V Strelkov; Stephen D Weeks
Journal: J Biol Chem Date: 2017-05-09 Impact factor: 5.157

The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture.

Review 1. Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.

2. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.

3. Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.

4. The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.

5. Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.

6. It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.

7. Mechanistic insights into the switch of αB-crystallin chaperone activity and self-multimerization.

8. Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif.

Review 9. One size does not fit all: the oligomeric states of αB crystallin.

Review 10. Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.