English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Like insulin-like growth factor binding protein-3 (IGFBP-3), IGFBP-5 was recently shown to form ternary complexes with insulin-like growth factor (IGF) and the acid-labile subunit (ALS). Previous studies using IGFBP-5/IGFBP-6 chimeric proteins have identified major and minor ALS binding sites in the carboxyl-terminal and central regions, respectively of IGFBP-5. We now report that ALS binds to IGFBP-3 (Ka = 1.1 ± 0.1 liters/nmol) and IGFBP-5 (Ka = 1.8 ± 0.5 liters/nmol) with similar binding affinities. Using site-specific mutants, we have identified residues K211/R214/K217/R218 within the carboxyl-terminal region of IGFBP-5 as being essential for ALS binding. Mutation of K134R136 or K138K139 in the central region of IGFBP-5 resulted in a small decrease in ALS binding.

Mutagenesis of Basic Amino Acids in the Carboxyl-Terminal Region of Insulin-Like Growth Factor Binding Protein-5 Affects Acid-Labile Subunit Binding