Document Detail


Aggregation-prone near-native intermediate formation during unfolding of a structurally similar non-lenticular βγ-crystallin domain.
MedLine Citation:
PMID:  23043265     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The folding-unfolding of structurally similar proteins belonging to a family have long been a focus of investigation for stating structure-(un)folding relationship. Such studies are yet to bring a consensus upon whether structurally similar domains follow common or different unfolding pathways. Members of βγ-crystallin superfamily which consists of structurally similar proteins with limited sequence similarity from diverse life forms spanning microbes to mammals, form appropriate model system to explore this relationship further. We selected a new member Crybg3_D3, the third βγ-crystallin domain of a non-lens vertebrate protein Crybg3 from mouse brain. The crystal structure solved at 1.86 Å demonstrates that βγ-crystallin domain of Crybg3 resembles more closely to the lens βγ-crystallins than the microbial crystallins do. However, interestingly, this structural cousin follows quite distinct (un)folding pathway via formation of intermediate state. The intermediate species is in native-like conformation with variation in flexibility and tends to form insoluble aggregates. The individual domains of lens βγ-crystallins (and microbial homologues) do not follow such an unfolding pattern. Thus, even the closest members of a sub-family within a superfamily do not necessarily follow similar unfolding paths, suggesting the divergence acquired by these domains, which could be observed only by unfolding. Additionally, this study provides insights into the modifications that this domain has undergone during its recruitment into the non-lens tissues in vertebrates.
Authors:
V Rajanikanth; Shanti Swaroop Srivastava; Aditya Kumar Singh; Meduri Rajyalakshmi; Kousik Chandra; Penmatsa Aravind; Rajan Sankaranarayanan; Yogendra Sharma
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-8
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-9     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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