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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Structure and functional analysis of the MYND domain
Roberta Spadaccini1, Hélène Perrin, Matthew J Bottomley
1EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Journal of Molecular Biology
|March 11, 2006
Summary
The MYND domain, a zinc binding motif, has a novel structure with two sequential zinc binding sites. This finding advances understanding of protein interactions in development and cancer.
Area of Science:
- Structural biology
- Molecular biology
- Biochemistry
Background:
- The MYND domain is a conserved zinc binding motif implicated in protein-protein interactions, crucial for transcriptional regulation, development, and cancer.
- Its structure and precise function in molecular interactions remain incompletely understood.
Purpose of the Study:
- To determine the three-dimensional structure of the MYND domain from human deformed epidermal autoregulatory factor-1 (DEAF-1).
- To characterize the novel zinc binding fold and its implications for protein interactions.
Main Methods:
- Three-dimensional structure determination of the DEAF-1 MYND domain using X-ray crystallography or NMR spectroscopy.
- Homology modeling of the BS69 MYND domain.
- Mutational analysis of the BS69 MYND domain.
Main Results:
- The DEAF-1 MYND domain adopts a novel zinc binding fold with two sequential zinc binding sites, distinct from other known zinc finger domains.
- This fold comprises a beta hairpin and two alpha helices, classifying it as a novel member of the treble-clef family of zinc binding domains.
- Mutational analysis of the related BS69 MYND domain identified crucial positively charged residues involved in molecular interactions, suggesting specificity is determined by surface charge.
Conclusions:
- The determined structure reveals a unique MYND domain fold with implications for its role in protein-protein interactions.
- Understanding MYND domain structure and binding specificities can provide insights into developmental processes and cancer mechanisms.
- Further research into MYND domain interactions may lead to novel therapeutic strategies.
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