 |
PDBsum entry 1ncv
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Determination of the three-Dimensional structure of cc chemokine monocyte chemoattractant protein 3 by 1h two-Dimensional nmr spectroscopy.
|
|
|
Authors
|
|
S.Meunier,
J.M.Bernassau,
J.C.Guillemot,
P.Ferrara,
H.Darbon.
|
|
|
Ref.
|
|
Biochemistry, 1997,
36,
4412-4422.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
MCP-3 is a beta chemokine consisting of 76 amino acid residues. It has been
described to be involved in the activation of all leukocytic cells, activation
mediated by the presence of multiple binding sites on the target cells. Its
three-dimensional structure has been studied by making use of two-dimensional 1H
NMR spectroscopy. MCP-3 exhibits the same monomeric structure as the other
chemokines, i.e., a three-stranded antiparallel beta sheet covered on one face
by an alpha helix. Although it belongs to the same subfamily as RANTES (Chung et
al., 1995; Faitbrother et al., 1994) and hMIP-1beta (Lodi et al., 1994), the
MCP-3 dimer is folded like IL-8 with the so-called alphabeta sandwich structural
motif. Structural and sequence analysis gives clear indications suggesting that
the other MCP chemokines may have the same quaternary structure, contrary to the
other beta chemokines.
|
|
|
|
|
|
|
