ArticleBiochemistry2009
Annexin I and annexin II N-terminal peptides binding to S100 protein family members: specificity and thermodynamic characterization.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Covalent Inhibitors of S100A4 Block the Formation of a Pro-Metastasis Non-Muscle Myosin 2A Complex.Journal of medicinal chemistry · 2024Article
- S100A6 Protein-Expression and Function in Norm and Pathology.International journal of molecular sciences · 2023Review
- Detection of human annexin A1 as the novel N-terminal tag for separation and purification handle.Microbial cell factories · 2023Article
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- The resealing factor S100A11 interacts with annexins and extended synaptotagmin-1 in the course of plasma membrane wound repair.Frontiers in cell and developmental biology · 2022Article
- Were Ancestral Proteins Less Specific?Molecular biology and evolution · 2021Article
- Expression of S100 proteins is associated with HBV intrauterine transmission.Archives of gynecology and obstetrics · 2020Article
- Learning peptide recognition rules for a low-specificity protein.Protein science : a publication of the Protein Society · 2020Article
- S100A11 protects against neuronal cell apoptosis induced by cerebral ischemia via inhibiting the nuclear translocation of annexin A1.Cell death & disease · 2018Article
- Conservation of Specificity in Two Low-Specificity Proteins.Biochemistry · 2018Article
- Article
- Annexin A2 complexes with S100 proteins: structure, function and pharmacological manipulation.British journal of pharmacology · 2015Review
- Investigation of neutrophilic peptides in periprosthetic tissue by matrix-assisted laser desorption ionisation time-of-flight imaging mass spectrometry.International orthopaedics · 2015Article
- Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin.Protein science : a publication of the Protein Society · 2014Article
- Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization.Biochemistry · 2013Article
- Article
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Design, synthesis, and structure-activity relationship exploration of 1-substituted 4-aroyl-3-hydroxy-5-phenyl-1H-pyrrol-2(5H)-one analogues as inhibitors of the annexin A2-S100A10 protein interaction.Journal of medicinal chemistry · 2011Article
- Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an α-helix.Biochemistry · 2011Article
- Modulation of quaternary structure of S100 proteins by calcium ions.Biophysical chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The S100 proteins make up a family of dimeric calcium binding proteins that function in response to changing calcium levels. Several S100 binding proteins have been identified; however, the exact biological functions of the S100 proteins are largely unknown as there are several factors which modulate their functions. To address these issues, the specificity of binding of representative members of the human S100 proteins to short N-terminal peptides of annexin I (AnI) and annexin II (AnII) was investigated under controlled experimental conditions. AnI and AnII have been shown previously to interact with S100A11 and S100A10, respectively. This provided a unique opportunity to determine their binding specificity with the other members of the human S100 protein family. It was found that AnI binds S100A6 or S100A11 while AnII binds S100A10 or S100A11. This is the first report of the interaction between S100A6 and AnI. The fact that AnI and AnII bind to selected members of the S100 protein family shows that these interactions are specific and that the mode of binding is different from that of calmodulin, as it was found not to bind AnI or AnII. From the analysis of the thermodynamics of interactions, the binding seems to be entropically driven. It was found that both AnI and AnII undergo a coil-to-helix transition upon binding to their respective binding partners. The observation that there is an overlap in functionality is not surprising due to considerable sequence homology between S100 protein family members. In fact, the functional overlap can explain previous failures of S100 knockout constructs to show any detectable changes in phenotype despite numerous implications of these proteins in important cellular processes.
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