Role of the N-terminus in the structure and stability of chicken annexin V.
The role of the short N-terminal region of chicken annexin V in the maintenance of the protein structure and its influence in the conformation of the calcium binding regions was analyzed. The N-terminal domain is not essential for protein folding, wild-type and dnt-annexin V showing almost identical secondary structures. However, the partial truncation of the N-terminus significantly decreases the melting temperature of the protein and induces the partial exposure of Trp187 which is normally located in a hydrophobic pocket of the calcium binding region of domain 3 of annexin V in the Ca2+-free form.
Arboledas
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Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense, Madrid, Spain.
Olmo
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N
Lizarbe
M A
MA
Turnay
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J
D000818:Animals; D017304:Annexin A5 / Q000096:biosynthesis / Q000737:chemistry*; D002645:Chickens; D002942:Circular Dichroism; D004355:Drug Stability; D006358:Hot Temperature; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017384:Sequence Deletion; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D017304:Annexin A5; D011994:Recombinant Proteins