1HFF

NMR solution structures of the vMIP-II 1-10 peptide from Kaposi's sarcoma-associated herpesvirus.

1HFF の概要

• エントリーDOI: 10.2210/pdb1hff/pdb
• 関連するPDBエントリー: 1CM9 1HFG 1VMP
• NMR情報: BMRB: 4914
• 分子名称: VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II (1 entity in total)
• 機能のキーワード: chemokine, cxcr4, anatagonist, vmip-ii
• 由来する生物種: HUMAN HERPESVIRUS 8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1169.31

構造登録者

Crump, M.P.,Elisseeva, E.,Gong, J.H.,Clark-Lewis, I.,Sykes, B.D. (登録日: 2000-12-01, 公開日: 2000-12-07, 最終更新日: 2024-05-15)

主引用文献

Crump, M.P.,Elisseeva, E.,Gong, J.H.,Clark-Lewis, I.,Sykes, B.D.
Structure/Function of Human Herpesvirus-8 Mip-II (1-71) and the Antagonist N-Terminal Segment (1-10)
FEBS Lett., 489:171-, 2001

PubMed Abstract: 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.

PubMed: 11165244
DOI: 10.1016/S0014-5793(00)02393-0

実験手法

SOLUTION NMR