1HHV
SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II
Summary for 1HHV
| Entry DOI | 10.2210/pdb1hhv/pdb |
| Descriptor | VIRUS CHEMOKINE VMIP-II (1 entity in total) |
| Functional Keywords | vmip-ii, virus chemokine, kshv(human herpesvirus 8), receptor binding, viral protein |
| Cellular location | Secreted: Q98157 |
| Total number of polymer chains | 1 |
| Total formula weight | 8462.80 |
| Authors | Shao, W.,Fernandez, E.,Navenot, J.M.,Wilken, J.,Thompson, D.A.,Pepiper, S.,Schweitzer, B.I.,Lolis, E. (deposition date: 1998-12-06, release date: 2003-09-16, Last modification date: 2024-10-30) |
| Primary citation | Shao, W.,Fernandez, E.,Sachpatzidis, A.,Wilken, J.,Thompson, D.A.,Schweitzer, B.I.,Lolis, E. CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure Eur.J.Biochem., 268:2948-2959, 2001 Cited by PubMed Abstract: Human herpesvirus-8 (HHV-8) is the infectious agent responsible for Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II (vMIP-II), which shows sequence similarity to the human CC chemokines. vMIP-II has broad receptor specificity that crosses chemokine receptor subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine receptors. In this study, the solution structure of chemically synthesized vMIP-II was determined by nuclear magnetic resonance. The protein is a monomer and possesses the chemokine fold consisting of a flexible N-terminus, three antiparallel beta strands, and a C-terminal alpha helix. Except for the N-terminal residues (residues 1-13) and the last two C-terminal residues (residues 73-74), the structure of vMIP-II is well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respectively. Taking into account the sequence differences between the various CC chemokines and comparing their three-dimensional structures allows us to implicate residues that influence the quaternary structure and receptor binding and activation of these proteins in solution. The analysis of the sequence and three-dimensional structure of vMIP-II indicates the presence of epitopes involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II was initially specific for CCR5 and acquired receptor-binding properties to CCR2 and other chemokine receptors. PubMed: 11358512DOI: 10.1046/j.1432-1327.2001.02184.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
