Implications of atomic-resolution structures for cell adhesion

Daniel J. Leahy

Research output: Contribution to journalReview articlepeer-review

Abstract

Molecules involved in cell adhesion processes are often both structurally and functionally modular, with subdomains that are members of large protein families. Recently, high-resolution structures have been determined for representative members of many of these families including fragments of integrins, cadherins, fibronectin-like domains, and immunoglobulin-like domains. These structures have enhanced our understanding of cell adhesion processes at several levels. In almost all cases, ligand- binding sites have been visualized and provide insight into how these molecules mediate biologically important interactions. Metal-binding sites have been identified and characterized, allowing assessment of the role of bound ions in cell adhesion processes. Many of these structures serve as templates for modeling homologous domains in other proteins or, when the structure of a fragment consisting of more than one domain is determined, the structure of multidomain arrays of homologous domains. Knowledge of atomic structure also allows rational design of drugs that either mimic or target specific binding sites. In many cases, high-resolution structures have revealed unexpected relationships that pose questions about the evolutionary origin of specific domains. This review briefly describes several recently determined structures of cell adhesion molecules, summarizes some of the main results of each structure, and highlights common features of different systems.

Original languageEnglish (US)
Pages (from-to)363-393
Number of pages31
JournalAnnual Review of Cell and Developmental Biology
Volume13
DOIs
StatePublished - Dec 1 1997

Keywords

  • Cadherin
  • Fibronectin
  • Immunoglobulin
  • Integrin

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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