1esr

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|PDB= 1esr |SIZE=350|CAPTION= <scene name='initialview01'>1esr</scene>, resolution 2.00&Aring;
|PDB= 1esr |SIZE=350|CAPTION= <scene name='initialview01'>1esr</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
|ACTIVITY=
|ACTIVITY=
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|DOMAIN=
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|RELATEDENTRY=[[1dok|1DOK]], [[1dol|1DOL]], [[1dom|1DOM]], [[1bo0|1BO0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1esr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esr OCA], [http://www.ebi.ac.uk/pdbsum/1esr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1esr RCSB]</span>
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:57 2008''

Revision as of 17:08, 30 March 2008


PDB ID 1esr

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Related: 1DOK, 1DOL, 1DOM, 1BO0


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN MONOCYTE CHEMOTACTIC PROTEIN-2


Overview

Monocyte chemotactic protein 2 (MCP-2) is a CC chemokine that utilizes multiple cellular receptors to attract and activate human leukocytes. MCP-2 is a potent inhibitor of HIV-1 by virtue of its high-affinity binding to the receptor CCR5, one of the major coreceptors for HIV-1. Although a few structures of CC chemokines have been reported, none of these was determined with the N-terminal pyroglutamic acid residue (pGlu1) and a complete C-terminus. pGlu1 is essential for the chemotactic activity of MCP-2. Recombinant MCP-2 has Gln1 at the N terminus, 12-15% of which cyclizes automatically and forms pGlu1. The chemotactic activity of such MCP-2 mixture, which contains 12-15% pGlu1-form and 85-88% Gln1-form protein, is approximately 10 times lower when compared with that of fully cyclized MCP-2 preparation. Therefore, this chemokine is practically inactive without pGlu1. We have determined the complete crystal structure of MCP-2 that contains both pGlu1 and an intact C-terminus. With the existence of pGlu1, the conformation of the N-terminus allows two additional interactions between the two subunits of MCP-2 dimer: a hydrogen bond between pGlu1 and Asn17 and a salt bridge between Asp3 and Arg18. Consequently, both pGlu1 are anchored and buried, and thereby, both N-terminal regions are protected against protease degradation. We have also observed not previously reported extended helical nature of the C terminal region, which covers residues 58-74.

About this Structure

1ESR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors., Blaszczyk J, Coillie EV, Proost P, Damme JV, Opdenakker G, Bujacz GD, Wang JM, Ji X, Biochemistry. 2000 Nov 21;39(46):14075-81. PMID:11087354

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