Chemokines from a structural perspective

Michelle C. Miller, Kevin H. Mayo

Research output: Contribution to journalReview articlepeer-review

57 Scopus citations

Abstract

Chemokines are a family of small, highly conserved cytokines that mediate various biological processes, including chemotaxis, hematopoiesis, and angiogenesis, and that function by interacting with cell surface G-Protein Coupled Receptors (GPCRs). Because of their significant involvement in various biological functions and pathologies, chemokines and their receptors have been the focus of therapeutic discovery for clinical intervention. There are several sub-families of chemokines (e.g., CXC, CC, C, and CX3C) defined by the positions of sequentially conserved cysteine residues. Even though all chemokines also have a highly conserved, three-stranded β-sheet/α-helix tertiary structural fold, their quarternary structures vary significantly with their sub-family. Moreover, their conserved tertiary structures allow for subunit swapping within and between sub-family members, thus promoting the concept of a “chemokine interactome”. This review is focused on structural aspects of CXC and CC chemokines, their functional synergy and ability to form heterodimers within the chemokine interactome, and some recent developments in structure-based chemokine-targeted drug discovery.

Original languageEnglish (US)
Article number2088
JournalInternational Journal of Molecular Sciences
Volume18
Issue number10
DOIs
StatePublished - Oct 2017

Bibliographical note

Publisher Copyright:
© 2017 by the authors. Licensee MDPI, Basel, Switzerland.

Keywords

  • Chemokine
  • Heterodimers
  • Interactome
  • NMR
  • Structure

PubMed: MeSH publication types

  • Journal Article
  • Review

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