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α-lactalbumin possesses a distinct zinc binding site

Abstract:

It has been proposed that the binding of Zn2+ to α-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human α-lactalbumin-Zn2+ complex at 1.7-Å resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of α-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This...

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
Journal:
Journal of Biological Chemistry
Volume:
268
Issue:
26
Pages:
19292-19298
Publication date:
1993-09-15
ISSN:
0021-9258
Source identifiers:
445037
Language:
English
Pubs id:
pubs:445037
UUID:
uuid:c0e5ff7c-0f4c-4b47-bd89-ce0a4eb03742
Local pid:
pubs:445037
Deposit date:
2014-10-29

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