1hfg

NMR solution structure of vMIP-II 1-71 from Kaposi's sarcoma-associated herpesvirus (minimized average structure).

spinqualitylabelsall models 1hfg, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hfg is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1hff, 1cm9, 1vmp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VMI2_HHV8P] Blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors. May form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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