1dol: Difference between revisions

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New page: left|200px<br /> <applet load="1dol" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dol, resolution 2.4Å" /> '''MONOCYTE CHEMOATTRAC...
 
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[[Image:1dol.gif|left|200px]]<br />
[[Image:1dol.gif|left|200px]]<br /><applet load="1dol" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dol" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dol, resolution 2.4&Aring;" />
caption="1dol, resolution 2.4&Aring;" />
'''MONOCYTE CHEMOATTRACTANT PROTEIN 1, I-FORM'''<br />
'''MONOCYTE CHEMOATTRACTANT PROTEIN 1, I-FORM'''<br />


==Overview==
==Overview==
The X-ray crystal structure of recombinant human monocyte chemoattractant, protein (MCP-1) has been solved in two crystal forms. One crystal form, (P), refined to 1.85 A resolution, contains a dimer in the asymmetric, unit, while the other (I) contains a monomer and was refined at 2.4 A., Although both crystal forms grow together in the same droplet, the, respective quaternary structures of the protein differ dramatically. In, addition, both X-ray structures differ to a similar extent from the, solution structure of MCP-1. Such extent of variability of quaternary, structures is unprecedented. In the crystal structures, the well-ordered N, termini of MCP-1 form 3(10)-helices. Comparison of the three MCP-1, structures revealed a direct correlation between the main-chain, conformation of the first two cysteine residues and the quaternary, arrangements. These data can be used to explain the structural basis for, the assignment of residues responsible for biological activity.
The X-ray crystal structure of recombinant human monocyte chemoattractant protein (MCP-1) has been solved in two crystal forms. One crystal form (P), refined to 1.85 A resolution, contains a dimer in the asymmetric unit, while the other (I) contains a monomer and was refined at 2.4 A. Although both crystal forms grow together in the same droplet, the respective quaternary structures of the protein differ dramatically. In addition, both X-ray structures differ to a similar extent from the solution structure of MCP-1. Such extent of variability of quaternary structures is unprecedented. In the crystal structures, the well-ordered N termini of MCP-1 form 3(10)-helices. Comparison of the three MCP-1 structures revealed a direct correlation between the main-chain conformation of the first two cysteine residues and the quaternary arrangements. These data can be used to explain the structural basis for the assignment of residues responsible for biological activity.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1DOL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOL OCA].  
1DOL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOL OCA].  


==Reference==
==Reference==
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[[Category: x-ray structure]]
[[Category: x-ray structure]]


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