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Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners
- Source :
- International Journal of Molecular Sciences, Vol 21, Iss 5879, p 5879 (2020), International Journal of Molecular Sciences
- Publication Year :
- 2020
- Publisher :
- MDPI AG, 2020.
-
Abstract
- Annexins and S100 proteins form two large families of Ca2+-binding proteins. They are quite different both structurally and functionally, with S100 proteins being small (10–12 kDa) acidic regulatory proteins from the EF-hand superfamily of Ca2+-binding proteins, and with annexins being at least three-fold larger (329 ± 12 versus 98 ± 7 residues) and using non-EF-hand-based mechanism for calcium binding. Members of both families have multiple biological roles, being able to bind to a large cohort of partners and possessing a multitude of functions. Furthermore, annexins and S100 proteins can interact with each other in either a Ca2+-dependent or Ca2+-independent manner, forming functional annexin-S100 complexes. Such functional polymorphism and binding indiscrimination are rather unexpected, since structural information is available for many annexins and S100 proteins, which therefore are considered as ordered proteins that should follow the classical “one protein–one structure–one function” model. On the other hand, the ability to be engaged in a wide range of interactions with multiple, often unrelated, binding partners and possess multiple functions represent characteristic features of intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs); i.e., functional proteins or protein regions lacking unique tertiary structures. The aim of this paper is to provide an overview of the functional roles of human annexins and S100 proteins, and to use the protein intrinsic disorder perspective to explain their exceptional multifunctionality and binding promiscuity.
- Subjects :
- 0301 basic medicine
Annexins
Review
protein–protein interactions
Intrinsically disordered proteins
S100 protein
Catalysis
Protein–protein interaction
Inorganic Chemistry
lcsh:Chemistry
03 medical and health sciences
annexin
0302 clinical medicine
multifunctionality
Annexin
Humans
Protein Interaction Maps
Physical and Theoretical Chemistry
Molecular Biology
lcsh:QH301-705.5
Spectroscopy
Functional polymorphism
Chemistry
S100 Proteins
Organic Chemistry
SUPERFAMILY
General Medicine
Ca2+-binding protein
intrinsically disordered protein
Computer Science Applications
Large cohort
Cell biology
Intrinsically Disordered Proteins
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
030220 oncology & carcinogenesis
Function (biology)
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 16616596 and 14220067
- Volume :
- 21
- Issue :
- 5879
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....1cc66687774ac7aa63b2b7077336a280