Dimerization and ion binding properties of S100P protein.
Functional S100P requires dimer formation and dimerization might form for one of the two reasons: i. producing a pair of sites for target protein binding or ii. modulation of cation binding affinity. The extent of exposed protein hydrophobicity was related to dimer formation.
Tutar
Yusuf
Y
Cumhuriyet Universitesi Kimya Bölümü Biyokimya A.B.D. Sivas Turkey. ytutar@cumhuriyet.edu.tr
D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D019281:Dimerization; D020832:EF Hand Motifs; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D009154:Mutation; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D002135:Calcium-Binding Proteins; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; C103003:S100P protein, human; D008274:Magnesium; D002118:Calcium