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Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1
Open accessAbstract
The three-dimensional structure of stromal cell-derived factor-1 (SDF-1) was determined by NMR spectroscopy. SDF-1 is a monomer with a disordered N-terminal region (residues 1-8), and differs from other chemokines in the packing of the hydrophobic core and surface charge distribution. Results with analogs showed that the N-terminal eight residues formed an important receptor binding site; however, only Lys-1 and Pro-2 were directly involved in receptor activation. Modification to Lys-1 and/or Pro-2 resulted in loss of activity, but generated potent SDF-1 antagonists. Residues 12-17 of the loop region, which we term the RFFESH motif, unlike the N-terminal region, were well defined in the SDF-1 structure. The RFFESH formed a receptor binding site, which we propose to be an important initial docking site of SDF-1 with its receptor. The ability of the SDF-1 analogs to block HIV-1 entry via CXCR4, which is a HIV-1 coreceptor for the virus in addition to being the receptor for SDF-1, correlated with their affinity for CXCR4. Activation of the receptor is not required for HIV-1 inhibition.
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“The protein product of CCL11 resulting from differential signal peptide cleavage is predicted to retain additional amino-acid residues at its N terminus, a key region specifying binding and activity of chemokines.44”
From Whole-genome sequencing suggests a chemokine gene cluster that modifies age at onset in familial Alzheimer's disease (2015) · cites this paper as [44]
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CXCL12-PLGA/Pluronic Nanoparticle Internalization Abrogates CXCR4-Mediated Cell Migration
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“Receptor interaction with CXCL12 was elucidated several years ago [13].”
BackgroundArmani-Tourret, M., Zhou, Z., Gasser, R., Staropoli, I., Cantaloube-Ferrieu, V., Bénureau, Y., García‐Pérez, J., Pérez‐Olmeda, M., Lorin, V., Puissant‐Lubrano, B., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009526 · Cited by 18
“As previously shown [43], P2G had a reduced anti-HIV-1 potency compared to CXCL12 (S4 Fig), presumably due to lack of CXCR4 endocytosis [23].”
BackgroundSelf-citationNMR structures of anti-HIV d-peptides derived from the N-terminus of viral chemokine vMIP-II
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“Similar to its human homologue, a typical ‘‘KPVSLSYRCPCRFFESH’’ sequence was also found at the N-terminal site of the tree shrew CXCL12 protein, and it is this conserved 17 aa domain that directly interacts with the receptor CXCR4 in humans [31].”
BackgroundThe marriage of chemokines and galectins as functional heterodimers
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“These concentrations were chosen to fully saturate CXCR4 binding, as they are many folds higher than the reported Kd for CXCR4/CXCL12 binding (∼4 nM) (57).”
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“Mutagenesis studies of chemokines in combination with structure determinations through nuclear magnetic resonance, crystallization, and molecular modeling revealed that the flexible N-terminal residues, including the N loop, a short fragment immediately after the first two conserved cysteines, are thought to be the pr…”
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“14 Lys1 of SDF-1, essential for the chemotactic activi ty towards CXCR4 [61], exhibits specific Hbond interactions with the -OH groups of Tyr112 (TM 3), Tyr251 (TM6), and Tyr262 (EL3), and”
The multilayered complexity of the chemokine receptor system
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Sulfotyrosine Recognition as Marker for Druggable Sites in the Extracellular Space
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“The N-terminal region of SDF-1 is involved in CXCR4 binding and activation (Crump et al., 1997).”
InfluentialHeckmann, D., Laufs, S., Maier, P. J., Zucknick, M., Giordano, F. A., Veldwijk, M. R., Eckstein, V., Wenz, F. K., Zeller, W. J., Früehauf, S., et al. (2011) · Oncology Research and Treatment · doi:10.1159/000332390 · Cited by 15
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“The protein missing the N-terminal lysine does not trigger receptor activation and a version without the eight N-terminal amino acids had significantly decreased receptor binding [20].”
Background
Metadata
- Authors
- Crump, M. P., Gong, J., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana‐Seisdedos, F., Virelizier, J., Baggiolini, M., Sykes, B. D., & Clark‐Lewis, I.
- Affiliations
- University of Alberta (CA)
- University of British Columbia (CA)
- University of Bern (CH)
- Institut Pasteur (FR)
- Corresponding author
- Sykes, Brian D.
- Clark‐Lewis, Ian
- Venue
- The EMBO Journal
- Published
- 1997-12-01
- Volume
- 16
- Issue
- 23
- Pages
- 6996-7007
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1170303
- OpenAlex
- W1964083898
- Cited by
- 731
- References
- 45
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 19 · 2023: 14 · 2022: 17 · 2021: 15 · 2020: 29 · 2019: 32 · 2018: 20 · 2017: 35 · 2016: 26 · 2015: 34 · 2014: 30 · 2013: 44 · 2012: 35
- FWCI
- 10.34
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council Canada
- Medical Research Council
- Topics
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- CXCL12, chemokine structure, N-terminal disordered region, receptor binding sites, CXCR4, HIV-1 coreceptor, HIV-1 entry inhibition, receptor activation, chemokine antagonists
- MeSH terms
- Amino Acid Sequence, Binding Sites, Models, Biological, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Structure-Activity Relationship, Virus Replication, HIV-1, Sequence Homology, Amino Acid, Chemokines, Anti-HIV Agents, Receptors, CXCR4, Chemokines, CXC, Nuclear Magnetic Resonance, Biomolecular, Chemokine CXCL12
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