ArticleBiophysical journal2002
Calcium-dependent conformational rearrangements and protein stability in chicken annexin A5.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Structures of annexin A2-PS DNA complexes show dominance of hydrophobic interactions in phosphorothioate binding.Nucleic acids research · 2023Article
- Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane.Molecules (Basel, Switzerland) · 2017Article
- In situ NMR measurement of macromolecule-bound metal ion concentrations.Journal of biomolecular NMR · 2016Article
- Quantitative analysis of annexin V-membrane interaction by flow cytometry.European biophysics journal : EBJ · 2015Article
- Annexin-phospholipid interactions. Functional implications.International journal of molecular sciences · 2013Article
- Conserved BK channel-protein interactions reveal signals relevant to cell death and survival.PloS one · 2011Article
- Key role of the N-terminus of chicken annexin A5 in vesicle aggregation.Protein science : a publication of the Protein Society · 2009Article
- Structure-function relationship in annexin A13, the founder member of the vertebrate family of annexins.The Biochemical journal · 2005Article
- Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study.Biophysical journal · 2004Article
- Structural and functional characterization of recombinant mouse annexin A11: influence of calcium binding.The Biochemical journal · 2003Article
- A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core.Journal of bacteriology · 2003Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conformational rearrangements that take place after calcium binding in chicken annexin A5 and a mutant lacking residues 3-10 were analyzed, in parallel with human annexin A5, by circular dichroism (CD), infrared spectroscopy (IR), and differential scanning calorimetry. Human and chicken annexins present a slightly different shape in the far-UV CD and IR spectra, but the main secondary-structure features are quite similar (70-80% alpha-helix). However, thermal stability of human annexin is significantly lower than its chicken counterpart (approximately 8 degrees C) and equivalent to the chicken N-terminally truncated form. The N-terminal extension contributes greatly to stabilize the overall annexin A5 structure. Infrared spectroscopy reveals the presence of two populations of alpha-helical structures, the canonical alpha-helices (approximately 1650 cm(-1)) and another, at a lower wavenumber (approximately 1634 cm(-1)), probably arising from helix-helix interactions or solvated alpha-helices. Saturation with calcium induces: alterations in the environment of the unique tryptophan residue of the recombinant proteins, as detected by near-UV CD spectroscopy; more compact tertiary structures that could account for the higher thermal stabilities (8 to 12 degrees C), this effect being higher for human annexin; and an increase in canonical alpha-helix percentage by a rearrangement of nonperiodical structure or 3(10) helices together with a variation in helix-helix interactions, as shown by amide I curve-fitting and 2D-IR.
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