1dok
From Proteopedia
(New page: 200px<br /> <applet load="1dok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dok, resolution 1.85Å" /> '''MONOCYTE CHEMOATTRA...) |
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| - | [[Image:1dok.gif|left|200px]]<br /> | + | [[Image:1dok.gif|left|200px]]<br /><applet load="1dok" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dok" size=" | + | |
caption="1dok, resolution 1.85Å" /> | caption="1dok, resolution 1.85Å" /> | ||
'''MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM'''<br /> | '''MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of recombinant human monocyte chemoattractant | + | 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== | ||
| - | 1DOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Boque, L.]] | [[Category: Boque, L.]] | ||
[[Category: Bujacz, G.]] | [[Category: Bujacz, G.]] | ||
| - | [[Category: Domaille, P | + | [[Category: Domaille, P J.]] |
| - | [[Category: Handel, T | + | [[Category: Handel, T M.]] |
[[Category: Lubkowski, J.]] | [[Category: Lubkowski, J.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:48 2008'' |
Revision as of 10:18, 21 February 2008
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MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM
Contents |
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.
Disease
Known diseases associated with this structure: Coronary artery disease, modifier of OMIM:[158105], HIV-1, resistance to OMIM:[158105], Mycobacterium tuberculosis, susceptibility to OMIM:[158105], Spina bifida, susceptiblity to OMIM:[158105]
About this Structure
1DOK is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions., Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A, Nat Struct Biol. 1997 Jan;4(1):64-9. PMID:8989326
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