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| ALPHA-LACTALBUMIN POSSESSES A DISTINCT ZINC-BINDING SITE |
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| Author(s): REN JS, STUART DI, ACHARYA KR |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 268 Issue: 26 Pages: 19292-19298 Published: SEP 15 1993 |
| Times Cited: 59 References: 42 |
| 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-angstrom 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 SO42- ion bound at the interface between three molecules. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV BATH, DEPT BIOCHEM, CLAVERTON DOWN, BATH BA2 7AY, AVON ENGLAND
2. LAB MOLEC BIOPHYS, OXFORD OX1 3QU, ENGLAND
3. OXFORD CTR MOLEC SCI, NEW CHEM LAB, OXFORD OX1 3QT, ENGLAND |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: LW819 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |