ArticleProceedings of the National Academy of Sciences of the United States of America1995
One sequence, two folds: a metastable structure of CD2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 73 citations in OpenAlex.
- Topological and Structural Plasticity of the Single Ig Fold and the Double Ig Fold Present in CD19.Biomolecules · 2021Article
- The metastable states of proteins.Protein science : a publication of the Protein Society · 2020Review
- Article
- Oocyte-triggered dimerization of sperm IZUMO1 promotes sperm-egg fusion in mice.Nature communications · 2015Article
- A Single Amino Acid in the Hinge Loop Region of the FOXP Forkhead Domain is Significant for Dimerisation.The protein journal · 2015Article
- An alternative conformation of the T-cell receptor alpha constant region.Journal of molecular biology · 2010Article
- Domain metastability: a molecular basis for immunoglobulin deposition?Journal of molecular biology · 2010Review
- The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters.The Journal of cell biology · 2009Article
- Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins bind through the same adhesive interface?Journal of molecular biology · 2008Article
- On the origin of the histone fold.BMC structural biology · 2007Article
- Peptide segments in protein-protein interfaces.Journal of biosciences · 2007Article
- Molecular mechanism of domain swapping in proteins: an analysis of slower motions.Biophysical journal · 2004Article
- 3D domain swapping: as domains continue to swap.Protein science : a publication of the Protein Society · 2002Review
- Stability and folding rates of domains spanning the large A-band super-repeat of titin.Biophysical journal · 2001Article
- Mechanical fatigue in repetitively stretched single molecules of titin.Biophysical journal · 2001Article
- Advances in the molecular characterization of tryptophan hydroxylase.Journal of molecular neuroscience : MN · 1998Review
- Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- 3D domain swapping: a mechanism for oligomer assembly.Protein science : a publication of the Protein Society · 1995Review
- When one and one are not two.Nature structural biology · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When expressed as part of a glutathione S-transferase fusion protein the NH2-terminal domain of the lymphocyte cell adhesion molecule CD2 is shown to adopt two different folds. The immunoglobulin superfamily structure of the major (85%) monomeric component has previously been determined by both x-ray crystallography and NMR spectroscopy. We now describe the structure of a second, dimeric, form present in about 15% of recombinant CD2 molecules. After denaturation and refolding in the absence of the fusion partner, dimeric CD2 is converted to monomer, illustrating that the dimeric form represents a metastable folded state. The crystal structure of this dimeric form, refined to 2.0-A resolution, reveals two domains with overall similarity to the IgSF fold found in the monomer. However, in the dimer each domain is formed by the intercalation of two polypeptide chains. Hence each domain represents a distinct folding unit that can assemble in two different ways. In the dimer the two domains fold around a hydrophilic interface believed to mimic the cell adhesion interaction at the cell surface, and the formation of dimer can be regulated by mutating single residues at this interface. This unusual misfolded form of the protein, which appears to result from inter- rather than intramolecular interactions being favored by an intermediate structure formed during the folding process, illustrates that evolution of protein oligomers is possible from the sequence for a single protein domain.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.