1esr
From Proteopedia
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| - | [[Image:1esr. | + | [[Image:1esr.jpg|left|200px]]<br /><applet load="1esr" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1esr" size=" | + | |
caption="1esr, resolution 2.00Å" /> | caption="1esr, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN MONOCYTE CHEMOTACTIC PROTEIN-2'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN MONOCYTE CHEMOTACTIC PROTEIN-2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ESR 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:// | + | 1ESR 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=1ESR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:44:49 2008'' |
Revision as of 13:44, 15 February 2008
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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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