1hml: Difference between revisions

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[[Image:1hml.gif|left|200px]]
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[[Image:1hml.png|left|200px]]


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{{STRUCTURE_1hml|  PDB=1hml  |  SCENE=  }}  
{{STRUCTURE_1hml|  PDB=1hml  |  SCENE=  }}  


'''ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE'''
===ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8366079}}


==About this Structure==
==About this Structure==
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[[Category: Stuart, D I.]]
[[Category: Stuart, D I.]]
[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
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Revision as of 05:24, 1 July 2008

File:1hml.png

Template:STRUCTURE 1hml

ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

Template:ABSTRACT PUBMED 8366079

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

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