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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Metals in protein-protein interfaces.

Woon Ju Song1, Pamela A Sontz, Xavier I Ambroggio

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093; emails: w6song@ucsd.edu , psontz@ucsd.edu , tezcan@ucsd.edu.

Annual Review of Biophysics
|April 30, 2014
PubMed
Summary
This summary is machine-generated.

Transition metal ions and metallocofactors are crucial in biology, often functioning at protein interfaces. These interfacial metals stabilize protein interactions, regulate signaling, and catalyze essential reactions, highlighting their significant biological roles.

Keywords:
interfacial metal clustersmetal-mediated oligomerizationmetal/metallocofactorsprotein self-assemblyprotein–protein interactions

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biometals

Background:

  • Transition metal ions and metallocofactors are vital for numerous biological processes, including global nutrient cycling and DNA processing.
  • While the interaction between metal ions and protein scaffolds is well-studied, their specific roles at protein-protein interfaces are often overlooked.

Purpose of the Study:

  • To provide a structural overview of transition metal ions and metallocofactors situated at protein-protein interfaces.
  • To highlight the diverse biological functions and importance of these interfacial metal centers through selected examples.

Main Methods:

  • Literature review and structural analysis of transition metal ions and metallocofactors in protein complexes.
  • Compilation of case studies illustrating the biological significance of metals at protein-protein interfaces.

Main Results:

  • Transition metals at protein interfaces are key to stabilizing protein-protein interactions, both permanent and transient.
  • These interfacial metals facilitate conformational changes in signaling complexes in response to stimuli.
  • They are essential catalysts for complex chemical reactions carried out by multisubunit protein assemblies.

Conclusions:

  • The location of transition metal ions and metallocofactors at protein-protein interfaces is critical for their biological function.
  • Understanding these interfacial metal centers provides insight into fundamental biological processes and potential therapeutic targets.