Amino acid sequence and crystal structure of buffalo α-lactalbumin

V. Calderone; M. G. Giuffrida; D. Viterbo; L. Napolitano; D. Fortunato; A. Conti; K. R. Acharya

doi:10.1016/0014-5793(96)00933-7

Amino acid sequence and crystal structure of buffalo α-lactalbumin

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

University of Bath
Ctro. Studi Alimentazione Animali C.
University of Turin

Research output: Contribution to journal › Article › peer-review

26 Citations (SciVal)

Abstract

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.

Original language	English
Pages (from-to)	91-95
Number of pages	5
Journal	FEBS Letters
Volume	394
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(96)00933-7
Publication status	Published - 23 Sept 1996

Funding

Acknowledgements." This work was supported by a Leverhulme Trust research grant to K.R.A. and the Italian MURST and the British Council (UK) travel grant to K.R.A. and A.C.V.C. is supported by the Italian MURST through a protein chemistry Ph.D. course grant.

Keywords

Amino acid sequence
Buffalo milk
Crystal structure
α-Lactalbumin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(96)00933-7

Cite this

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abstract = "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 {\AA} 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.",

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AU - Giuffrida, M. G.

AU - Viterbo, D.

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AU - Fortunato, D.

AU - Conti, A.

AU - Acharya, K. R.

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Amino acid sequence and crystal structure of buffalo α-lactalbumin

Abstract

Funding

Keywords

ASJC Scopus subject areas

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