The atomic structure of protein-protein recognition sites.
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Summary
An analysis of the atomic structure of the recognition sites seen in 75 protein-protein complexes of known three-dimensional structure shows that atoms buried at protein- protein interfaces are close-packed like the protein interior.
- Type
- review
- Published
- 1999-02-05
- Cited by
- 1,971
- References
- 135
- OpenAlex
- https://openalex.org/W2075770210
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20154946
Keywords
Crystallography, Chemistry, Polar, Protein structure, Macromolecule
References
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- Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibit
- Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin.
- The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen.
- Evaluation of mutagenesis for epitope mapping. Structure of an antibody-protein antigen complex.
- The structure of protein-protein recognition sites.
- Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.
- Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.
- Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
- Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation.
- The structure of crystalline profilinβ-actin
- The 2.2 Å crystal structure of transducin-α complexed with GTPγS
- Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
- Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution.
- The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution
- Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution.
- Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
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- Protein-Protein Interactions in Receptor Activation and Intracellular Signalling
- Solvent accessibility of the thrombin-thrombomodulin interface.
- Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle.
- Statistical analysis of atomic contacts at RNA–protein interfaces
- Electrostatic contributions to protein–protein interactions: Fast energetic filters for docking and their physical basis
- Inhibition of trypsin by cowpea thionin: Characterization, molecular modeling, and docking
- CAPRI: A Critical Assessment of PRedicted Interactions
- Structural studies of FocB and Transthyretin
- Atomic contact vectors in protein‐protein recognition
- Fluctuations and Entropy in The Energetics and Function of Protein Complexes
- The Structural GDP/GTP Cycle of Rab11 Reveals a Novel Interface Involved in the Dynamics of Recycling Endosomes*
- ProMate: a structure based prediction program to identify the location of protein-protein binding sites.
- Apolipoprotein E‐low density lipoprotein receptor binding: Study of protein–protein interaction in rationally selected docked complexes
- Structure and function of the double-strand break repair machinery.
- Chemical Basis for the Affinity Maturation of a Camel Single Domain Antibody*
- Localization and Characterization of Flavivirus Envelope Glycoprotein Cross-Reactive Epitopes
- Strong in Vivo Maturation Compensates for Structurally Restricted H3 Loops in Antibody Repertoires*
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