Amino acid sequence and crystal structure of buffalo α‐lactalbumin

FEBS Letters

Acharya, K.R.²  Napolitano, L.³  Fortunato, D.³  Calderone, V.²  Viterbo, D.¹  Giuffrida, M.G.³  Conti, A.³ 

[1] Department of Inorganic, Physical and Materials Chemistry, University of Turin, Turin, Italy;School of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK;Centro Studi Alimentazione Animali CNR, Turin, Italy

关键词: Amino acid sequence;    Crystal structure;    α-Lactalbumin;    Buffalo milk;   

DOI  :  10.1016/0014-5793(96)00933-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo α-lactalbumin were performed in order to gain further knowledge of the molecular basis of α-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine α-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 Å is very similar to those previously reported for human and baboon α-lactalbumins. However, a portion of the molecule (residues 105–109) exhibits different conformation. It forms a ‘flexible loop’, and appears to be a functionally important region in forming the lactose synthase complex.

【 授权许可】

Unknown