Interface interactions between βγ-crystallin domain and Ig-like domain render Ca2+ -binding site inoperative in abundant perithecial protein of Neurospora crassa-Reference-Cited by-同舟云学术

Interface interactions between βγ-crystallin domain and Ig-like domain render Ca2+ -binding site inoperative in abundant perithecial protein of Neurospora crassa

Published:2018-10-16 Issue:6 Volume:110 Page:955-972
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Swaroop Srivastava Shanti¹,Raman Rajeev¹,Kiran Uday¹,Garg Rupsi¹,Chadalawada Swathi¹,Pawar Asmita D.¹,Sankaranarayanan Rajan¹²,Sharma Yogendra¹²^ORCID

Affiliation:

1. CSIR - Centre for Cellular and Molecular Biology (CCMB); Hyderabad 500 007 India

2. Academy of Scientific and Innovative Research (AcSIR); New Delhi India

Funder

Department of Biotechnology , Ministry of Science and Technology

Science and Engineering Research Board

Council for Scientific and Industrial Research

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/mmi.14130/fullpdf

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1. Chemical Properties Determine Solubility and Stability in βγ‐Crystallins of the Eye Lens;ChemBioChem;2021-02-10

2. βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca 2+ -Dependent Activity Modulation;Journal of Bacteriology;2019-12

3. Abundant Perithecial Protein (APP) from Neurospora is a primitive functional analog of ocular crystallins;Biochemical and Biophysical Research Communications;2019-08