Alpha-lactalbumin possesses a distinct zinc binding site.
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 an...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1993
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| _version_ | 1797060470222356480 |
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| author | Ren, J Stuart, D Acharya, K |
| author_facet | Ren, J Stuart, D Acharya, K |
| author_sort | Ren, J |
| collection | OXFORD |
| description | 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 lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules. |
| first_indexed | 2024-03-06T20:17:35Z |
| format | Journal article |
| id | oxford-uuid:2ca8c68b-badc-4df0-aced-e8ea1a6c1458 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:17:35Z |
| publishDate | 1993 |
| record_format | dspace |
| spelling | oxford-uuid:2ca8c68b-badc-4df0-aced-e8ea1a6c14582022-03-26T12:38:30ZAlpha-lactalbumin possesses a distinct zinc binding site.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2ca8c68b-badc-4df0-aced-e8ea1a6c1458EnglishSymplectic Elements at Oxford1993Ren, JStuart, DAcharya, KIt 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 lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules. |
| spellingShingle | Ren, J Stuart, D Acharya, K Alpha-lactalbumin possesses a distinct zinc binding site. |
| title | Alpha-lactalbumin possesses a distinct zinc binding site. |
| title_full | Alpha-lactalbumin possesses a distinct zinc binding site. |
| title_fullStr | Alpha-lactalbumin possesses a distinct zinc binding site. |
| title_full_unstemmed | Alpha-lactalbumin possesses a distinct zinc binding site. |
| title_short | Alpha-lactalbumin possesses a distinct zinc binding site. |
| title_sort | alpha lactalbumin possesses a distinct zinc binding site |
| work_keys_str_mv | AT renj alphalactalbuminpossessesadistinctzincbindingsite AT stuartd alphalactalbuminpossessesadistinctzincbindingsite AT acharyak alphalactalbuminpossessesadistinctzincbindingsite |