User:Coline Perrin/CCL2

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(New page: ==Introduction== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> The''' chemokine (C-C motif) ligand''' (CCL2), also known as : - monoc...)
Current revision (12:15, 27 January 2016) (edit) (undo)
 
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==Introduction==
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<StructureSection load='1dok' size='350' side='right' caption='Monocyte chemoattractant protein 1 (PDB code [[3idf]])' scene='72/721520/Cv/2'>
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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== Function and Structure ==
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The''' chemokine (C-C motif) ligand''' (CCL2), also known as :
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- monocyte chemotactic protein 1 (MCP1)
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'''Human synthetic monocyte chemoattractant protein 1 (MCP)''' belongs to the superfamily of chemokines, which are proteins involved in immunoregulatory and inflammatory processes. The gene for CCL2 is on chromosome 17 in region 17q11.2-q12. The superfamily can be subdivided into 4 smaller groups, depending on the N-ter arangment of the cysteines. The CCL2<ref>PMID:8170963</ref> is also known as '''chemokine (C-C motif) ligand''' or:
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- MCP1
- small inducible cytokine A2 (SCYA2)
- small inducible cytokine A2 (SCYA2)
- MCAF
- MCAF
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- GDCF-2
- GDCF-2
- HC11.
- HC11.
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== Function ==
 
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== Disease ==
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It exists as a monomer or a dimer, eventhough the homodimer form is preferred.
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The structure of the monomer is made of <scene name='72/721520/Ligand_binding_on_ccl2/2'>3 Beta sheets and 1 alpha helix</scene>.
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== Ligands ==
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The known ligands for CCL2 are <scene name='72/721520/Ligand_binding_on_ccl2/1'>Potassium and PO4</scene>. The potassium binds to the S33 and S34 of the monomer and PO4 binds to F15 and N17.
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== Relevance ==
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/if/3ifd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Diseases ==
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CCL2 is implicated in several diseases like psoriasis and rheumatoid arthritis where the appear to recruit macrophages, therefore bolstering the inflammation on joints.
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It is thought to be involved in atherosclerosis in the recruitment of monocytes into the arterial wall as well as in prostate cancer<ref>PMID:25917126</ref>.
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It has also been found elevated in the urine of people with lupus as a sign warning of inflammation of the kidney.
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CCL2 is overexpressed in epilepsy, brain ischemia, Alzheimer's disease, EAE and traumatic brain injury.
== Structural highlights ==
== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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CCL2 is part of the C-C motif group because of the covalent bond made between <scene name='72/721520/Cv/4'>2 of the 4 cysteines of the N terminal domain</scene>.<ref>PMID:8989326</ref>
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<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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Post translational modifications at the N-terminus can regulate receptor and target cell selectivity. Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant.
</StructureSection>
</StructureSection>
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[[Image:chaine.png]]
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== Synthesis ==
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The protein human CCL2 has been synthesized using a combination of solid phase peptide synthesis (SPPS) and native chemical ligation (NCL). The thioester-peptide segment was synthesized using the sulfonamide safety-catch linker and 9-fluorenylmethoxycarbonyl (Fmoc) SPPS, and pseudoproline dipeptides were used to facilitate the synthesis of both CCL2 fragments. After assembly of the full-length peptide chain by NCL, a glutathione redox buffer was used to fold and oxidize the CCL2 protein.
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CCL2 was crystallized and the structure was determined by X-ray diffraction at 1.9-A resolution. This is probably one of the first crystal structures of a protein prepared using the sulfonamide safety-catch linker and NCL.
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==3D structures of Monocyte chemoattractant protein==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* Monocyte chemoattractant protein 1
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**[[1dok]], [[1dol]] – hMCP-1 (mutant) - human<br />
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**[[3ifd]] – hMCP-1 <br />
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**[[1dom]], [[1don]] – hMCP-1 - NMR<br />
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**[[1ml0]], [[2nz1]] – hMCP-1 (mutant) + M3 protein<br />
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**[[2bdn]] – hMCP-1 + antibody<br />
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**[[4dn4]] – hMCP-1 (mutant) + antibody<br />
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**[[4zk9]] – hMCP-1 + chemokine binding protein<br />
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**[[4r8i]] – hMCP-1 + RNA<br />
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* Monocyte chemoattractant protein 2
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**[[1esr]] – hMCP-2 (mutant) <br />
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* Monocyte chemoattractant protein 3
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**[[1ncv]], [[1bo0]] – hMCP-3 - NMR<br />
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**[[4zkc]] – hMCP-3 + chemokine binding protein<br />
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* Monocyte chemoattractant protein 4
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**[[2ra4]] – hMCP-4 <br />
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}}
== References ==
== References ==
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https://fr.wikipedia.org/wiki/CCL2
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http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1DOK
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http://www.uniprot.org/uniprot/P13500#interaction
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http://www.rcsb.org/pdb/explore/explore.do?structureId=3IFD
<references/>
<references/>

Current revision

Monocyte chemoattractant protein 1 (PDB code 3idf)

Drag the structure with the mouse to rotate

Image:chaine.png

Synthesis

The protein human CCL2 has been synthesized using a combination of solid phase peptide synthesis (SPPS) and native chemical ligation (NCL). The thioester-peptide segment was synthesized using the sulfonamide safety-catch linker and 9-fluorenylmethoxycarbonyl (Fmoc) SPPS, and pseudoproline dipeptides were used to facilitate the synthesis of both CCL2 fragments. After assembly of the full-length peptide chain by NCL, a glutathione redox buffer was used to fold and oxidize the CCL2 protein. CCL2 was crystallized and the structure was determined by X-ray diffraction at 1.9-A resolution. This is probably one of the first crystal structures of a protein prepared using the sulfonamide safety-catch linker and NCL.

3D structures of Monocyte chemoattractant protein

Updated on 27-January-2016

References

https://fr.wikipedia.org/wiki/CCL2 http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1DOK http://www.uniprot.org/uniprot/P13500#interaction http://www.rcsb.org/pdb/explore/explore.do?structureId=3IFD

  1. ↑ Carr MW, Roth SJ, Luther E, Rose SS, Springer TA. Monocyte chemoattractant protein 1 acts as a T-lymphocyte chemoattractant. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3652-6. PMID:8170963
  2. ↑ Ito Y, Ishiguro H, Kobayashi N, Hasumi H, Watanabe M, Yao M, Uemura H. Adipocyte-derived monocyte chemotactic protein-1 (MCP-1) promotes prostate cancer progression through the induction of MMP-2 activity. Prostate. 2015 Jul 1;75(10):1009-19. doi: 10.1002/pros.22972. Epub 2015 Apr 27. PMID:25917126 doi:http://dx.doi.org/10.1002/pros.22972
  3. ↑ Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions. Nat Struct Biol. 1997 Jan;4(1):64-9. PMID:8989326

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Coline Perrin

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