Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family - PubMed (original) (raw)

Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family

James W Murphy et al. Proteins. 2010 Apr.

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Figures

Figure 1

Figure 1

Phylogenetic tree calculated using the neighbor-joining (NJ) method representing all human chemokines and their isoforms. The tree is based on the multiple sequence alignment. The three isoforms of CXCL12 (SDF-1α, β, and γ) are indicated at the uppermost portion of the figure.

Figure 2

Figure 2

Crystal structures of CXCL12. (a) Cartoon representation of the single protein chain of the asymmetric unit in the P3221 space group CXCL12 crystals. Chemokine structural elements are labeled. (b) The protein composition of the asymmetric unit in the P212121 space group CXCL12 crystals. Ten monomers are arranged as an elongated decamer and form five CC-like dimers. (c) The semi-transparent surface representation of the asymmetric unit of the P3221 space group of CXCL12 and a symmetry mate forms a CXC dimer that interact through their α-helices and β-strand-1. (d) Semi-transparent surface of two representative chains in the decamer of CXCL12 which form a CC chemokine-like dimer and interact with their amino termini and 30’s loops. (e) CXC dimer of CXCL12 (upper panel) compared to CC dimer of CXCL12 (lower panel). Both dimers were aligned using only Chain A of each in the alignment algorithm.

Figure 3

Figure 3

Intersubunit contacts of CXCL12 dimers. (a) Arginine zipper motif forms the interactions in the amino terminal regions of the CC-like CXCL12 dimer. Cysteines are colored yellow, arginines from chains A and B are colored purple and red, respectively. (b) Crystallographic packing between CC-dimers. Cartoon representation with semi-transparent surface of two representative chains in the decamer of CXCL12 in between each CC chemokine-like dimer. (c) Overlay of the CC-like dimer of CXCL12 and the CC dimer of CCL5. Chain A from each dimer was aligned. Glutamic acid 15 from CXCL12 and isoleucine 15 from CCL5 are shown as sticks to indicate the 180° rotation of the carbon backbone.

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References

    1. Rot A, von Andrian UH. Chemokines in innate and adaptive host defense: basic chemokinese grammar for immune cells. Annu Rev Immunol. 2004;22:891–928. - PubMed
    1. Veldkamp CT, Ziarek JJ, Su J, Basnet H, Lennertz R, Weiner JJ, Peterson FC, Baker JE, Volkman BF. Monomeric structure of the cardioprotective chemokine SDF-1/CXCL12. Protein Science. 2009;18(7):1359–1369. - PMC - PubMed
    1. Viola A, Luster AD. Chemokines and Their Receptors: Drug Targets in Immunity and Inflammation. Annual Review of Pharmacology and Toxicology. 2008;48(1):171–197. - PubMed
    1. Fernandez EJ, Wilken J, Thompson DA, Peiper SC, Lolis E. Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation. Biochemistry. 2000;39(42):12837–12844. - PubMed
    1. Siciliano SJ, Rollins TE, DeMartino J, Konteatis Z, Malkowitz L, Van Riper G, Bondy S, Rosen H, Springer MS. Two-site binding of C5a by its receptor: an alternative binding paradigm for G protein-coupled receptors. Proc Natl Acad Sci U S A. 1994;91(4):1214–1218. - PMC - PubMed

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