Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Protein-protein interaction at crystal contacts

J Janin1, F Rodier

  • 1Laboratoire de Biologie Structurale, CNRS-Université Paris-Sud, Gif-sur-Yvette, France.

Proteins
|December 1, 1995
PubMed
Summary

Crystal packing contacts, though artifacts, reveal insights into nonspecific protein-protein interactions. These interactions bury less surface area than specific biological interactions, offering a comparative model.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Polyomavirus Large T Antigen Interact with the DISC and Protect against Fas Induced Apoptosis.

TheScientificWorldJournal·2018
Same author

Accumulation of sucrose in vacuoles isolated from red beet tissue.

Planta·2014
Same author

Mitochondrial DNA damage induces apoptosis in senescent cells.

Cell death & disease·2013
Same author

Chronic antiplatelet therapy and mortality among patients with infective endocarditis.

Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2009
Same author

A new protein-protein docking scoring function based on interface residue properties.

Bioinformatics (Oxford, England)·2007
Same author

Encapsulation of mono- and oligo-nucleotides into aqueous-core nanocapsules in presence of various water-soluble polymers.

International journal of pharmaceutics·2006

Area of Science:

  • Structural Biology
  • Biochemistry
  • Crystallography

Background:

  • Crystal packing contacts are non-specific interactions arising during protein crystallization.
  • These contacts utilize forces similar to those governing specific protein-protein recognition.
  • Understanding these nonspecific interactions provides a valuable comparison to biologically relevant protein associations.

Purpose of the Study:

  • To quantify and characterize pairwise interfaces in protein crystal structures.
  • To compare the surface area buried by nonspecific crystal contacts versus specific biological interactions.
  • To investigate the influence of crystallographic symmetry on interface formation.

Main Methods:

  • Analysis of 152 crystal forms containing monomeric proteins in the asymmetric unit.
  • Evaluation of the number and size of pairwise interfaces.
  • Comparison of interface areas with random simulations and known specific protein complexes.

Main Results:

  • Monomeric proteins in crystals without 2-fold symmetry form 8-10 pairwise interfaces, burying up to 4400 Ų.
  • Nonspecific pairwise interfaces bury 200-1200 Ų, smaller than specific interfaces in protease-inhibitor or antigen-antibody complexes (>1500 Ų).
  • Crystal forms with 2-fold symmetry exhibit fewer, larger interfaces (1500-2500 Ų), forming 'crystal oligomers'.

Conclusions:

  • Specific protein-protein interactions involve larger buried surface areas than nonspecific crystal contacts.
  • Crystal oligomers formed in the presence of 2-fold symmetry may reflect solution-state interactions.
  • Crystal packing provides a model system for studying forces relevant to biological protein associations.

Related Experiment Videos