1hml
From Proteopedia
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[[Image:1hml.gif|left|200px]] | [[Image:1hml.gif|left|200px]] | ||
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'''ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE''' | '''ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE''' | ||
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[[Category: Ren, J.]] | [[Category: Ren, J.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
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Revision as of 16:01, 2 May 2008
ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
Overview
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.
About this Structure
1HML is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Alpha-lactalbumin possesses a distinct zinc binding site., Ren J, Stuart DI, Acharya KR, J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079 Page seeded by OCA on Fri May 2 19:01:06 2008