Antigen Specificity and High Affinity Binding Provided by One Single Loop of a Camel Single-domain Antibody
Open Access
- 1 July 2001
- journal article
- Published by Elsevier BV
- Vol. 276 (28), 26285-26290
- https://doi.org/10.1074/jbc.m102107200
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?Journal of Molecular Biology, 2000
- Camel heavy-chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen-binding repertoireThe EMBO Journal, 2000
- Structural determinants in the sequences of immunoglobulin variable domainJournal of Molecular Biology, 1998
- Conformations of the third hypervariable region in the VH domain of immunoglobulinsJournal of Molecular Biology, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Structural Biology, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Structural Biology, 1994
- Three-dimensional structure of an Fv from a human IgM immunoglobulinJournal of Molecular Biology, 1992
- Structural repertoire of the human VH segmentsJournal of Molecular Biology, 1992
- Canonical structures for the hypervariable regions of immunoglobulinsJournal of Molecular Biology, 1987
- Domain association in immunoglobulin molecules: The packing of variable domainsJournal of Molecular Biology, 1985