1hff
From Proteopedia
(New page: 200px<br /><applet load="1hff" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hff" /> '''NMR SOLUTION STRUCTURES OF THE VMIP-II 1-10 ...) |
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caption="1hff" /> | caption="1hff" /> | ||
'''NMR SOLUTION STRUCTURES OF THE VMIP-II 1-10 PEPTIDE FROM KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS.'''<br /> | '''NMR SOLUTION STRUCTURES OF THE VMIP-II 1-10 PEPTIDE FROM KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Kaposi's sarcoma-associated herpesvirus encodes a chemokine called vMIP-II | + | Kaposi's sarcoma-associated herpesvirus encodes a chemokine called vMIP-II that has been shown to be a broad range human chemokine receptor antagonist. Two N-terminal peptides, vMIP-II(1-10) and vMIP-II(1-11)dimer (dimerised through Cys11) were synthesised. Both peptides are shown to bind the CXC chemokine receptor 4 (CXCR4). vMIP-II(1-10) was 1400-fold less potent than the native protein whilst the vMIP-II(1-11)dimer was only 180-fold less potent. In addition, both peptides are CXCR4 antagonists. Through analysis of non-standard, long mixing time two-dimensional nuclear Overhauser enhancement spectroscopy experiments, 13C relaxation data and amide chemical shift temperature gradients for the N-terminus of vMIP-II, we show that this region populates a turn-like structure over residues 5-8, both in the presence and absence of the full protein scaffold. This major conformation is likely to be in fast exchange with other conformational states but it has not previously been detected in monomeric chemokine structures. This and other studies [Elisseeva et al. (2000) J. Biol. Chem. 275, 26799-26805] suggest that there may be a link between the structuring of the short N-terminal chemokine peptides and their ability to bind their receptor. |
==About this Structure== | ==About this Structure== | ||
| - | 1HFF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 1HFF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clark-Lewis, I.]] | [[Category: Clark-Lewis, I.]] | ||
| - | [[Category: Crump, M | + | [[Category: Crump, M P.]] |
[[Category: Elisseeva, E.]] | [[Category: Elisseeva, E.]] | ||
| - | [[Category: Gong, J | + | [[Category: Gong, J H.]] |
| - | [[Category: Sykes, B | + | [[Category: Sykes, B D.]] |
[[Category: anatagonist]] | [[Category: anatagonist]] | ||
[[Category: chemokine]] | [[Category: chemokine]] | ||
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[[Category: vmip-ii]] | [[Category: vmip-ii]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:44 2008'' |
Revision as of 11:00, 21 February 2008
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NMR SOLUTION STRUCTURES OF THE VMIP-II 1-10 PEPTIDE FROM KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS.
Overview
Kaposi's sarcoma-associated herpesvirus encodes a chemokine called vMIP-II that has been shown to be a broad range human chemokine receptor antagonist. Two N-terminal peptides, vMIP-II(1-10) and vMIP-II(1-11)dimer (dimerised through Cys11) were synthesised. Both peptides are shown to bind the CXC chemokine receptor 4 (CXCR4). vMIP-II(1-10) was 1400-fold less potent than the native protein whilst the vMIP-II(1-11)dimer was only 180-fold less potent. In addition, both peptides are CXCR4 antagonists. Through analysis of non-standard, long mixing time two-dimensional nuclear Overhauser enhancement spectroscopy experiments, 13C relaxation data and amide chemical shift temperature gradients for the N-terminus of vMIP-II, we show that this region populates a turn-like structure over residues 5-8, both in the presence and absence of the full protein scaffold. This major conformation is likely to be in fast exchange with other conformational states but it has not previously been detected in monomeric chemokine structures. This and other studies [Elisseeva et al. (2000) J. Biol. Chem. 275, 26799-26805] suggest that there may be a link between the structuring of the short N-terminal chemokine peptides and their ability to bind their receptor.
About this Structure
1HFF is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Structure/function of human herpesvirus-8 MIP-II (1-71) and the antagonist N-terminal segment (1-10)., Crump MP, Elisseeva E, Gong J, Clark-Lewis I, Sykes BD, FEBS Lett. 2001 Feb 2;489(2-3):171-5. PMID:11165244
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