How electrostatic networks modulate specificity and stability of collagen

Hongning Zheng, Cheng Lu, Jun Lan, Shilong Fan, Vikas Nanda, Fei Xu

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


One-quarter of the 28 types of natural collagen exist as heterotrimers. The oligomerization state of collagen affects the structure and mechanics of the extracellular matrix, providing essential cues to modulate biological and pathological processes. A lack of highresolution structural information limits our mechanistic understanding of collagen heterospecific self-assembly. Here, the 1.77-Å resolution structure of a synthetic heterotrimer demonstrates the balance of intermolecular electrostatics and hydrogen bonding that affects collagen stability and heterospecificity of assembly. Atomistic simulations and mutagenesis based on the solved structure are used to explore the contributions of specific interactions to energetics. A predictive model of collagen stability and specificity is developed for engineering novel collagen structures.

Original languageEnglish (US)
Pages (from-to)6207-6212
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number24
StatePublished - Jun 12 2018

All Science Journal Classification (ASJC) codes

  • General


  • Cooperativity
  • Molecular dynamics
  • Protein design
  • Self-assembly
  • Triple helix


Dive into the research topics of 'How electrostatic networks modulate specificity and stability of collagen'. Together they form a unique fingerprint.

Cite this