- 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
- Journal:
- The Journal of biological chemistry
- Volume:
- 268
- Issue:
- 26
- Pages:
- 19292-19298
- Publication date:
- 1993-09-05
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:2ca8c68b-badc-4df0-aced-e8ea1a6c1458
- Source identifiers:
-
28016
- Local pid:
- pubs:28016
- Language:
- English
- Keywords:
- Copyright date:
- 1993
Journal article
Alpha-lactalbumin possesses a distinct zinc binding site.
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