1bg5: Difference between revisions

Revision as of 12:54, 21 February 2008

CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE

OverviewOverview

The ankyrin 33-residue repeating motif, an L-shaped structure with protruding beta-hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and alpha-Na,K-ATPase, a ubiquitous membrane protein critical to vectorial transport of ions and nutrients, is required to assemble and stabilize Na,K-ATPase at the plasma membrane. alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (AnkG, a product of the ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its second cytoplasmic domain. Fusion peptides of glutathione S-transferase incorporating these 25 amino acids bind specifically to purified ankyrin (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double beta-strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests that the valency and specificity of ankyrin binding is achieved by the interaction of 5-7-residue surface loops with the beta-hairpin tips of multiple ankyrin repeat units.

About this StructureAbout this Structure

1BG5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the ankyrin-binding domain of alpha-Na,K-ATPase., Zhang Z, Devarajan P, Dorfman AL, Morrow JS, J Biol Chem. 1998 Jul 24;273(30):18681-4. PMID:9668035

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-[[Image:1bg5.gif|left|200px]]<br /><applet load="1bg5" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1bg5, resolution 2.60&Aring;" />
 '''CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE'''<br />
 ==Overview==
-The ankyrin 33-residue repeating motif, an L-shaped structure with, protruding beta-hairpin tips, mediates specific macromolecular, interactions with cytoskeletal, membrane, and regulatory proteins. The, association between ankyrin and alpha-Na,K-ATPase, a ubiquitous membrane, protein critical to vectorial transport of ions and nutrients, is required, to assemble and stabilize Na,K-ATPase at the plasma membrane., alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1, gene) and Madin-Darby canine kidney cell ankyrin (AnkG, a product of the, ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its, second cytoplasmic domain. Fusion peptides of glutathione S-transferase, incorporating these 25 amino acids bind specifically to purified ankyrin, (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this, minimal ankyrin-binding motif, crystallized as the fusion protein, reveals, a 7-residue loop with one charged hydrophilic face capping a double, beta-strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests, that the valency and specificity of ankyrin binding is achieved by the, interaction of 5-7-residue surface loops with the beta-hairpin tips of, multiple ankyrin repeat units.
+The ankyrin 33-residue repeating motif, an L-shaped structure with protruding beta-hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and alpha-Na,K-ATPase, a ubiquitous membrane protein critical to vectorial transport of ions and nutrients, is required to assemble and stabilize Na,K-ATPase at the plasma membrane. alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (AnkG, a product of the ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its second cytoplasmic domain. Fusion peptides of glutathione S-transferase incorporating these 25 amino acids bind specifically to purified ankyrin (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double beta-strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests that the valency and specificity of ankyrin binding is achieved by the interaction of 5-7-residue surface loops with the beta-hairpin tips of multiple ankyrin repeat units.
 ==About this Structure==
-BG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA].
+BG5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Devarajan, P.]]
-[[Category: Morrow, J.S.]]
+[[Category: Morrow, J S.]]
 [[Category: Zhang, Z.]]
 [[Category: ankyrin binding]]
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 [[Category: ion transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:37:25 2007''
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