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New page: left|200px<br /><applet load="1wy9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wy9, resolution 2.10Å" /> '''Crystal structure of...
 
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[[Image:1wy9.gif|left|200px]]<br /><applet load="1wy9" size="450" color="white" frame="true" align="right" spinBox="true"  
[[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==
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.
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==
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].  
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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