Journal article icon

Journal article

Alpha-lactalbumin possesses a distinct zinc binding site.

Abstract:

It has been proposed that the binding of Zn2+ to alpha-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 alpha-lactalbumin-Zn2+ complex at 1.7-A 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 alpha-lactalbumin (the region which forms the active site of the homologous protein lys...

Expand abstract
Publication status:
Published

Actions


Authors


More by this author
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:
1993-09-01
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
28016
Language:
English
Keywords:
Pubs id:
pubs:28016
UUID:
uuid:2ca8c68b-badc-4df0-aced-e8ea1a6c1458
Local pid:
pubs:28016
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP