SAM Domains in Health and Diseases: Structural and Functional Insights
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biophysics: Structure, Dynamics, and Function".
Deadline for manuscript submissions: 31 March 2026
Special Issue Editors
Interests: structural biology; conformational analysis of proteins and peptides by NMR; evaluation of protein–protein and protein–peptide interactions by NMR; design and evaluation of inhibitors of protein–protein interactions; structure-based drug design; molecular modeling; docking; SAM domains
Special Issues, Collections and Topics in MDPI journals
Interests: structural biology; solution NMR: conformational analyses of proteins, peptides; self-assembling peptides: structural analyses; solution NMR: interaction studies [(protein–protein (PPIs)/protein–ligand (=peptides and small molecules) interactions]; NMR techniques in drug discovery; design and evaluation of PPI modulators; structure-based drug design; molecular modelling and docking; Sam domains; EphA2 receptor; cancer
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
SAM (Sterile Alpha Motif) domains represent small protein-interaction modules included in a variety of proteins from yeast to humans. They are characterized by a common three-dimensional organization made up of a five-helix bundle, but, despite structure similarity, they are capable of great binding versatility. In fact, a few SAM domains form oligomers and/or polymers through homo- and heterotypic SAM-SAM associations and others can even bind proteins lacking a SAM domain. In addition, interactions between certain SAM domains and nucleic acids or lipids have been reported. The binding heterogeneity characterizing SAM domains brings functional versatility. In fact, SAM domains participate in diverse physiological and pathological mechanisms through several signalling pathways, regulation of gene transcription, and cytoskeletal organization. SAM domain mutations and consequent dysfunctions have been often linked to diverse types of diseases such as cancer, cataracts, and neurological disorders. A few SAM-SAM interactions have been clearly connected to cancer. A deeper understanding at the molecular level of SAM domain-mediated pathological functions and targeted drug discovery campaigns are needed.
We are pleased to invite contributions to the Special Issue “SAM Domains in Health and Diseases: Structural and Functional Insights”.
In this Special Issue, original research articles and reviews, focused on the biological and structural properties of SAM domains and their involvement in physiological or pathological cell functions, are welcome. Multidisciplinary studies combining in silico and experimental work are highly desired.
We look forward to receiving your contributions.
Dr. Flavia Anna Mercurio
Dr. Marilisa Leone
Guest Editors
Manuscript Submission Information
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Keywords
- SAM domains
- oligomer- and polymer-forming SAM
- mid-loop/end-helix architecture of binding
- SAM physiological and pathological signaling pathways
- SAM domains as drug targets
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