1hyn: Difference between revisions

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[[Image:1hyn.gif|left|200px]]
{{Seed}}
[[Image:1hyn.png|left|200px]]


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{{STRUCTURE_1hyn|  PDB=1hyn  |  SCENE=  }}  
{{STRUCTURE_1hyn|  PDB=1hyn  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN'''
===CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN===




==Overview==
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The red blood cell membrane (RBCM) is a primary model for animal cell plasma membranes. One of its major organizing centers is the cytoplasmic domain of band 3 (cdb3), which links multiple proteins to the membrane. Included among its peripheral protein ligands are ankyrin (the major bridge to the spectrin-actin skeleton), protein 4. 1, protein 4.2, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphofructokinase, deoxyhemoglobin, p72syk protein tyrosine kinase, and hemichromes. The crystal structure of cdb3 is reported at 0.26 nm (2.6 A) resolution. A tight symmetric dimer is formed by cdb3; it is stabilized by interlocked dimerization arms contributed by both monomers. Each subunit also includes a larger peripheral protein binding domain with an alpha(+) beta-fold. The binding sites of several peripheral proteins are localized in the structure, and the nature of the major conformational change that regulates membrane-skeletal interactions is evaluated. An improved structural definition of the protein network at the inner surface of the RBCM is now possible.
The line below this paragraph, {{ABSTRACT_PUBMED_11049968}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11049968}}


==About this Structure==
==About this Structure==
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[[Category: Zhang, D.]]
[[Category: Zhang, D.]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
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