Canonical antigen-binding loop structures in immunoglobulins: More structures, more canonical classes?

Journal of Molecular Biology

Volumn 300, Issue 1, 2000, Pages 83-91

  Decanniere, K ^a   Muyldermans, S ^a   Wyns, L ^a  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

Author keywords

Antibody engineering; Antibody structure; Hypervariable loop; Single domain antibody

Indexed keywords

ANTIBODY; CHORIONIC GONADOTROPIN; IMMUNOGLOBULIN;

ALGORITHM; AMINO ACID SEQUENCE; ANTIBODY STRUCTURE; ANTIGEN BINDING; ARTICLE; ARTIODACTYLA; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENETIC ENGINEERING; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ARTIODACTYLA; CAMELUS DROMEDARIUS; LAMA GLAMA; MURINAE;

EID: 0034733379     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3839     Document Type: Article

References (40)

1. Standard conformations for the canonical structures of immunoglobulins
2. The differences between the structural repertoires of VII germ-line gene segments of mice and humans: Implication for the molecular mechanism of the immune response
3. Structural conservation of hypervariable regions in immunoglobulin evolution
4. Structure of antibody hypervariable loops reproduced by a conformational search algorithm
5. Canonical structures for the hypervariable regions of immunoglobulins
6. Conformations of immunoglobulin variable regions
7. Structural repertoire of the human VII segments
8. Structural determinants in the sequences of immunoglobulin variable domain
9. 'Camelising' human antibody fragments: NMR studies on VH domains
10. Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved protein stability
11. A single domain antibody fragment in complex with RNase A: Non-canonical loop structures and nanomolar affinity using two CDR loops
12. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
13. Selection an didentification of single-domain antibody fragments from camel heavy-chain antibodies
14. Naturally occurring antibodies devoid of light chains
15. Crystallographic structure studies of an IgG molecule and an Fc fragment
16. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
17. Enhanced conformational diversity search of CDR-H3 in antibodies: Role of the first CDR-H3 residue
18. Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
19. Modeling antibody hypervariable loops: A combined algorithm
20. Accessing the Kabat antibody sequence database by computer
21. Structural families in loops of homologous proteins: Automatic classification, modelling and application to antibodies
22. Conformations of the third hypervariable region in the VH domain of immunoglobulins
23. Sequence and structure of VH domain from naturally occurring camel heavy-chain immunoglobulins lacking light chains
24. Unique single-domain antigen binding fragments derived from naturally occuring camel heavy-chains antibodies
25. Camel heavy-chain antibodies: Diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
26. Anatomy of the antibody molecule
27. X-ray crystallography of antibodies
28. Reshaping human antibodies for therapy
29. Rearrangements of the former VL interface in the solution structure of a camelised, single antibody VH domain
30. Automatic classification of antibody complementarity-determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure prediction
31. Structural classification of CDR-H3 in antibodies
32. Conformational sampling of CDR-H3 in antibodies by multicanonical molecular dynamics simulation
33. H3-rules: Identification of CDR-H3 structures in antibodies
34. The crystal structure of a llama heavy chain variable domain
35. Camelid heavy-chain variable domains provide efficient combining sites to haptens
36. The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops
37. Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins
38. Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate
39. Comparison of llama VH sequences from conventional and heavy chain antibodies