ArticleProceedings of the National Academy of Sciences of the United States of America2004
Protein dynamics and the immunological evolution of molecular recognition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Antibody Polyreactivity: A Challenger of Immune Paradigms.Immunology · 2025Review
- Selective Recognition of Carbohydrate Antigens by Germline Antibodies Isolated from AID Knockout Mice.Journal of the American Chemical Society · 2022Article
- Redesigning an antibody H3 loop by virtual screening of a small library of human germline-derived sequences.Scientific reports · 2021Article
- Inference of Joint Conformational Distributions from Separately Acquired Experimental Measurements.The journal of physical chemistry letters · 2021Article
- Comparison of Huggins Coefficients and Osmotic Second Virial Coefficients of Buffered Solutions of Monoclonal Antibodies.Polymers · 2021Article
- Structure and Dynamics of Stacking Interactions in an Antibody Binding Site.Biochemistry · 2019Article
- Hybrid Refinement of Heterogeneous Conformational Ensembles Using Spectroscopic Data.The journal of physical chemistry letters · 2019Article
- Breaking the law: unconventional strategies for antibody diversification.Nature reviews. Immunology · 2019Review
- Refinement of Highly Flexible Protein Structures using Simulation-Guided Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Deciphering evolution of immune recognition in antibodies.BMC structural biology · 2018Article
- The Unusual Genetics and Biochemistry of Bovine Immunoglobulins.Advances in immunology · 2018Article
- Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification.Frontiers in immunology · 2018Article
- Therapeutic Antibodies to Ganglioside GD2 Evolved from Highly Selective Germline Antibodies.Cell reports · 2017Article
- Flexibility and Design: Conformational Heterogeneity along the Evolutionary Trajectory of a Redesigned Ubiquitin.Structure (London, England : 1993) · 2017Article
- Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies.Structure (London, England : 1993) · 2016Article
- Selection on protein structure, interaction, and sequence.Protein science : a publication of the Protein Society · 2016Review
- Probing the Impact of Local Structural Dynamics of Conformational Epitopes on Antibody Recognition.Biochemistry · 2016Article
- Methyl Relaxation Measurements Reveal Patterns of Fast Dynamics in a Viral RNA-Directed RNA Polymerase.Biochemistry · 2015Article
- Adaptive mutations alter antibody structure and dynamics during affinity maturation.Biochemistry · 2015Article
- Prevalence and gene characteristics of antibodies with cofactor-induced HIV-1 specificity.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While it is accepted that protein flexibility plays a role in protein folding, catalysis, and molecular recognition, few techniques are capable of the rigorous measurement of protein motions required to quantify flexibility. Three-pulse photon echo shift spectroscopy can be used to measure the time scale of protein motions, and we have used this technique, along with steady-state spectroscopy and binding and structural data, to examine the immunological evolution of protein flexibility in an anti-fluorescein antibody. Two light chain somatic mutations increase affinity for fluorescein by 12-fold but also significantly affect flexibility. Specifically, a rigidification of the protein is seen in each of three observable motions; two slower motions undergo decreased amplitudes of displacement, by 3- and 20-fold, respectively, in response to an applied force, and the distribution associated with the amplitude of a faster motion is narrowed upon somatic mutation. The somatic mutations appear to rigidify the antibody-fluorescein complex by more strongly anchoring fluorescein to the protein and by more tightly packing the complex. The data demonstrate that in addition to affinity, antibody dynamics are systematically manipulated during affinity maturation, and they imply that the evolution of protein flexibility may be a central component of the immune response. The results also reflect the type of protein rigidification that may be important for other biological interactions, such as protein-protein, protein-ligand or protein-drug, and enzyme-substrate recognition.
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