title: Amino acid sequence and crystal structure of buffalo alpha-lactalbumin.
abstract: Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo alpha-lactalbumin were performed in order to gain further knowledge of the molecular basis of alpha-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine alpha-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 A is very similar to those previously reported for human and baboon alpha-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.
authors.affiliation: School of Biology and Biochemistry, University of Bath, UK.
authors.forename: V
authors.initials: V
authors.lastname: Calderone
authors.forename: M G
authors.initials: MG
authors.lastname: Giuffrida
authors.forename: D
authors.initials: D
authors.lastname: Viterbo
authors.forename: L
authors.initials: L
authors.lastname: Napolitano
authors.forename: D
authors.initials: D
authors.lastname: Fortunato
authors.forename: A
authors.initials: A
authors.lastname: Conti
authors.forename: K R
authors.initials: KR
authors.lastname: Acharya
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002020:Buffaloes; D002845:Chromatography; D018360:Crystallography, X-Ray; D007768:Lactalbumin / Q000737:chemistry* / Q000302:isolation & purification; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
chemical_list: D007768:Lactalbumin