Motifs involved in protein-protein interactions
Identifieur interne : 004702 ( Main/Merge ); précédent : 004701; suivant : 004703Motifs involved in protein-protein interactions
Auteurs : C. Slingsby [Royaume-Uni] ; O. A. Bateman [Royaume-Uni] ; A. Simpson [Royaume-Uni]Source :
- Molecular Biology Reports [ 0301-4851 ] ; 1993-04-01.
English descriptors
- KwdEn :
- Teeft :
- Amino acids, Antiparallel strands, Barrel axes, Biol, Catalytic domain, Constant domains, Crystal structure, Cubic symmetry, Different orientation, Different subunits, Dihydrolipoyl transacetylase, Dimer, Dimer axis, Dimer formation, Dimer interface, Domain, Edge strands, Extracellular domain, First helix, Helix, Helix bundle, Helix bundles, Human growth hormone, Human growth hormone receptor, Hydrophobic side chains, Identical subunits, Immunoglobulin, Interface, Interface interactions, Intermolecular contacts, Linker region, Long axes, Long loop, Loop regions, Monomer, Oligomer, Polypeptide, Protein domains, Protein structure, Protein structures, Pseudo axis, Receptor, Rotation axis, Sandwich structure, Strand, Subunit, Symmetrical assemblies, Tandem domains, Topology, Trends biochem, Twofold axis, Variable domains.
Abstract
Summary: Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces.
Url:
DOI: 10.1007/BF00986727
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ISTEX:EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7Le document en format XML
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<term>interface</term>
<term>motif</term>
<term>oligomer</term>
<term>β-sheet</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Amino acids</term>
<term>Antiparallel strands</term>
<term>Barrel axes</term>
<term>Biol</term>
<term>Catalytic domain</term>
<term>Constant domains</term>
<term>Crystal structure</term>
<term>Cubic symmetry</term>
<term>Different orientation</term>
<term>Different subunits</term>
<term>Dihydrolipoyl transacetylase</term>
<term>Dimer</term>
<term>Dimer axis</term>
<term>Dimer formation</term>
<term>Dimer interface</term>
<term>Domain</term>
<term>Edge strands</term>
<term>Extracellular domain</term>
<term>First helix</term>
<term>Helix</term>
<term>Helix bundle</term>
<term>Helix bundles</term>
<term>Human growth hormone</term>
<term>Human growth hormone receptor</term>
<term>Hydrophobic side chains</term>
<term>Identical subunits</term>
<term>Immunoglobulin</term>
<term>Interface</term>
<term>Interface interactions</term>
<term>Intermolecular contacts</term>
<term>Linker region</term>
<term>Long axes</term>
<term>Long loop</term>
<term>Loop regions</term>
<term>Monomer</term>
<term>Oligomer</term>
<term>Polypeptide</term>
<term>Protein domains</term>
<term>Protein structure</term>
<term>Protein structures</term>
<term>Pseudo axis</term>
<term>Receptor</term>
<term>Rotation axis</term>
<term>Sandwich structure</term>
<term>Strand</term>
<term>Subunit</term>
<term>Symmetrical assemblies</term>
<term>Tandem domains</term>
<term>Topology</term>
<term>Trends biochem</term>
<term>Twofold axis</term>
<term>Variable domains</term>
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<front><div type="abstract" xml:lang="en">Summary: Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces.</div>
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