1wy9

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(New page: 200px<br /><applet load="1wy9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wy9, resolution 2.10&Aring;" /> '''Crystal structure of...)
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[[Image:1wy9.gif|left|200px]]<br /><applet load="1wy9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wy9, resolution 2.10&Aring;" />
caption="1wy9, resolution 2.10&Aring;" />
'''Crystal structure of microglia-specific protein, Iba1'''<br />
'''Crystal structure of microglia-specific protein, Iba1'''<br />
==Overview==
==Overview==
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The ionized calcium-binding adaptor molecule 1 (Iba1) with 147 amino acid, residues has been identified as a calcium-binding protein, expressed, specifically in microglia/macrophages, and is expected to be a key factor, in membrane ruffling, which is a typical feature of activated microglia., We have determined the crystal structure of human Iba1 in a Ca(2+)-free, form and mouse Iba1 in a Ca(2+)-bound form, to a resolution of 1.9 A and, 2.1 A, respectively. X-ray structures of Iba1 revealed a compact, single-domain protein with two EF-hand motifs, showing similarity in, overall topology to partial structures of the classical EF-hand proteins, troponin C and calmodulin. In mouse Iba1, the second EF-hand contains a, bound Ca(2+), but the first EF-hand does not, which is often the case in, S100 proteins, suggesting that Iba1 has S100 protein-like EF-hands. The, molecular conformational change induced by Ca(2+)-binding of Iba1 is, different from that found in the classical EF-hand proteins and/or S100, proteins, which demonstrates that Iba1 has an unique molecular switching, mechanism dependent on Ca(2+)-binding, to interact with target molecules.
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The ionized calcium-binding adaptor molecule 1 (Iba1) with 147 amino acid residues has been identified as a calcium-binding protein, expressed specifically in microglia/macrophages, and is expected to be a key factor in membrane ruffling, which is a typical feature of activated microglia. We have determined the crystal structure of human Iba1 in a Ca(2+)-free form and mouse Iba1 in a Ca(2+)-bound form, to a resolution of 1.9 A and 2.1 A, respectively. X-ray structures of Iba1 revealed a compact, single-domain protein with two EF-hand motifs, showing similarity in overall topology to partial structures of the classical EF-hand proteins troponin C and calmodulin. In mouse Iba1, the second EF-hand contains a bound Ca(2+), but the first EF-hand does not, which is often the case in S100 proteins, suggesting that Iba1 has S100 protein-like EF-hands. The molecular conformational change induced by Ca(2+)-binding of Iba1 is different from that found in the classical EF-hand proteins and/or S100 proteins, which demonstrates that Iba1 has an unique molecular switching mechanism dependent on Ca(2+)-binding, to interact with target molecules.
==About this Structure==
==About this Structure==
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1WY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WY9 OCA].
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1WY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY9 OCA].
==Reference==
==Reference==
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[[Category: ef-hand]]
[[Category: ef-hand]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:44:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:19 2008''

Revision as of 13:49, 21 February 2008


1wy9, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of microglia-specific protein, Iba1

Overview

The ionized calcium-binding adaptor molecule 1 (Iba1) with 147 amino acid residues has been identified as a calcium-binding protein, expressed specifically in microglia/macrophages, and is expected to be a key factor in membrane ruffling, which is a typical feature of activated microglia. We have determined the crystal structure of human Iba1 in a Ca(2+)-free form and mouse Iba1 in a Ca(2+)-bound form, to a resolution of 1.9 A and 2.1 A, respectively. X-ray structures of Iba1 revealed a compact, single-domain protein with two EF-hand motifs, showing similarity in overall topology to partial structures of the classical EF-hand proteins troponin C and calmodulin. In mouse Iba1, the second EF-hand contains a bound Ca(2+), but the first EF-hand does not, which is often the case in S100 proteins, suggesting that Iba1 has S100 protein-like EF-hands. The molecular conformational change induced by Ca(2+)-binding of Iba1 is different from that found in the classical EF-hand proteins and/or S100 proteins, which demonstrates that Iba1 has an unique molecular switching mechanism dependent on Ca(2+)-binding, to interact with target molecules.

About this Structure

1WY9 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding., Yamada M, Ohsawa K, Imai Y, Kohsaka S, Kamitori S, J Mol Biol. 2006 Dec 1;364(3):449-57. Epub 2006 Sep 15. PMID:17011575

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