Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface

Protein Science

Volumn 9, Issue 9, 2000, Pages 1852-1855

  Pokkuluri, P R ^a   Cai, X ^a   Johnson, G ^a   Stevens, F J ^a   Schiffer, M ^a  

^a ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Antibody light chain; Association constant; Crystal structure; Dimer interface; Quaternary interactions

Indexed keywords

ANTIBODY; DIMER; IMMUNOGLOBULIN LIGHT CHAIN; MUTANT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIMERIZATION; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE;

EID: 0033820074     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.9.1852     Document Type: Article

References (20)

1. The free R value: A more objective statistic for crystallography
2. Crystallography and NMR system: A new software system for macromolecular structure determination
3. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0 A resolution
4. SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
5. Protein stabilization by removal of unsatisfied polar groups: Computational approaches and experimental tests
6. Comparison of crystal structures of two homologous proteins: Structural origin of altered domain interactions in immunoglobulin light-chain dimers
7. Variable domain structure of the nonpathological human κIV light chain Len: High homology to the murine light chain McPC603
8. Solvent accessibility of groups in proteins
9. Satisfying hydrogen bonding potential in proteins
10. AMoRE: An automated package for molecular replacement
11. Protein folding and association: Insights from the interracial and thermodynamic properties of hydrocarbons
12. A domain flip as a result of a single amino-acid substitution
13. Reengineering immunoglobulin domain interactions by introduction of charged residues
14. CHAIN - A crystallographic modeling program
15. 0, the major structural protein of peripheral nerve myelin
16. Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
17. Analysis of protein-protein interaction by simulation of small-zone size-exclusion chromatography: Application to an antibody-antigen association
18. Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins
19. Hydrogen bonds and salt bridges across protein-protein interfaces