ArticleProtein science : a publication of the Protein Society2006
Backbone dynamics of SDF-1alpha determined by NMR: interpretation in the presence of monomer-dimer equilibrium.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 37 citations in OpenAlex.
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- The chemokine X-factor: Structure-function analysis of the CXC motif at CXCR4 and ACKR3.The Journal of biological chemistry · 2020Article
- Diflunisal targets the HMGB1/CXCL12 heterocomplex and blocks immune cell recruitment.EMBO reports · 2019Article
- Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study.Molecules (Basel, Switzerland) · 2018Article
- The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions.The Journal of biological chemistry · 2017Article
- Structural basis for chemokine recognition by a G protein-coupled receptor and implications for receptor activation.Science signaling · 2017Article
- Mutational Analysis of Atypical Chemokine Receptor 3 (ACKR3/CXCR7) Interaction with Its Chemokine Ligands CXCL11 and CXCL12.The Journal of biological chemistry · 2017Article
- New paradigms in chemokine receptor signal transduction: Moving beyond the two-site model.Biochemical pharmacology · 2016Review
- Structure-Based Identification of Novel Ligands Targeting Multiple Sites within a Chemokine-G-Protein-Coupled-Receptor Interface.Journal of medicinal chemistry · 2016Article
- The role of tyrosine sulfation in the dimerization of the CXCR4:SDF-1 complex.Protein science : a publication of the Protein Society · 2013Article
- Structural and functional consequences of the cardiac troponin C L48Q Ca(2+)-sensitizing mutation.Biochemistry · 2012Article
- Secreted CXCL12 (SDF-1) forms dimers under physiological conditions.The Biochemical journal · 2012Article
- Structural and biophysical insights into the ligand-free Pitx2 homeodomain and a ring dermoid of the cornea inducing homeodomain mutant.Biochemistry · 2012Article
- NMR in the Analysis of Functional Chemokine Interactions and Drug Discovery.Drug discovery today. Technologies · 2012Article
- Exploring platelet chemokine antimicrobial activity: nuclear magnetic resonance backbone dynamics of NAP-2 and TC-1.Antimicrobial agents and chemotherapy · 2011Article
- Oligomerization of a retroviral matrix protein is facilitated by backbone flexibility on nanosecond time scale.The journal of physical chemistry. B · 2011Article
- Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family.Proteins · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SDF-1alpha is a member of the chemokine family implicated in various reactions in the immune system. The interaction of SDF-1alpha with its receptor, CXCR4, is responsible for metastasis of a variety of cancers. SDF-1alpha is also known to play a role in HIV-1 pathogenesis. The structures of SDF-1alpha determined by NMR spectroscopy have been shown to be monomeric while X-ray structures are dimeric. Biochemical data and in vivo studies suggest that dimerization is likely to be important for the function of chemokines. We report here the dynamics of SDF-1alpha determined through measurement of main chain (15)N NMR relaxation data. The data were obtained at several concentrations of SDF-1alpha and used to determine a dimerization constant of approximately 5 mM for a monomer-dimer equilibrium. The dimerization constant was subsequently used to extrapolate values for the relaxation data corresponding to monomeric SDF-1alpha. The experimental relaxation data and the extrapolated data for monomeric SDF-1alpha were analyzed using the model free approach. The model free analysis indicated that SDF-1alpha is rigid on the nano- to picosecond timescale with flexible termini. Several residues involved in the dimer interface display slow micro- to millisecond timescale motions attributable to chemical exchange such as monomer-dimer equilibrium. NMR relaxation measurements are shown to be applicable for studying oligomerization processes such as the dimerization of SDF-1alpha.
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