March 1, 2004Journal of Biological ChemistryOpen Access

The SANT2 Domain of the Murine Tumor Cell DnaJ-like Protein 1 Human Homologue Interacts with α1-Antichymotrypsin and Kinetically Interferes with Its Serpin Inhibitory Activity

View Full Paper

Ask AI

Bookmark

Population

In vitro models and yeast two-hybrid screening studying the human homologue HTJ1 and alpha1-antichymotrypsin

Design

Preclinical

Authors

BKBarbara KroczyńskaNorthwestern University CEChristina M. Evangelista SSShalaka SamantUniversity of Illinois Urbana-Champaign

Discussion

Member takes

Implication

Hypothesis-generating for HTJ1-SANT2 modulation of ACT; should not yet alter clinical serpin-targeted strategies.

Structured PICO

Population

In vitro models and yeast two-hybrid screening studying the human homologue HTJ1 (of murine MTJ1/ERdj1) and alpha1-antichymotrypsin (ACT)

Intervention

SANT2 domain of HTJ1 (wild-type and single tryptophan-alanine substitutions)

Outcome

Protein-protein interaction between SANT2 domain and ACT, and effect on ACT inhibitory activity toward chymotrypsinsurrogate

The SANT2 domain of HTJ1 mediates stable, high-affinity protein-protein interactions with alpha1-antichymotrypsin, kinetically interfering with its serpin inhibitory activity.

Cite This Study

Kroczyńska et al. (2004) studied this question.

synapsesocial.com/papers/6a72bb6b35aa2c282ce367ba https://doi.org/10.1074/jbc.m310903200

View Full Paper

Ask AI

Bookmark

The SANT2 Domain of the Murine Tumor Cell DnaJ-like Protein 1 Human Homologue Interacts with α1-Antichymotrypsin and Kinetically Interferes with Its Serpin Inhibitory Activity

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The SANT2 Domain of the Murine Tumor Cell DnaJ-like Protein 1 Human Homologue Interacts with α1-Antichymotrypsin and Kinetically Interferes with Its Serpin Inhibitory Activity

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider