| URL: | http://agknapp.chemie.fu-berlin.de/bivalbind |
| Full name: | database for bi- and multivalent protein-ligand complexes. |
| Description: | Bival-Bind is a public, web-accessible database that contains 9153 crystal structures of bi- and multivalent protein-ligand complexes. Each of these complexes contains at least two ligands of the same type. Detailed information about the protein surface in between each possible pair of ligands has been generated and can be accessed through this web page. The database allows to descriminate between convex and concave topologies in between the ligand binding pockets. |
| Year founded: | 2014 |
| Last update: | |
| Version: | |
| Accessibility: |
Accessible
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| Country/Region: | Germany |
| Data type: | |
| Data object: |
NA
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| Database category: | |
| Major species: |
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| Keywords: |
| University/Institution: | Free University of Berlin |
| Address: | Department of Biology Chemistry, Pharmacy / Institute of Chemistry and Biochemistry, Free University of Berlin,, Berlin, Germany |
| City: | |
| Province/State: | |
| Country/Region: | Germany |
| Contact name (PI/Team): | ErnstâWalter Knapp |
| Contact email (PI/Helpdesk): | knapp@chemie.fu-berlin.de |
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Database of protein complexes with multivalent binding ability: Bival-Bind. [PMID: 24264865]
Phenomena of multivalent binding of ligands with receptors are ubiquitous in biology and of growing interest in material sciences. Multivalency can enhance binding affinity dramatically. To understand the mechanism of multivalent binding in more detail model systems of bi- and multivalent receptors are needed, but are difficult to find. Furthermore it is useful to know about multivalent receptors, which can serve as targets to design multivalent drugs. The present contribution tries to close this gap. The Bival-Bind database (http://agknapp.chemie.fu-berlin.de/bivalbind) provides a relatively complete list - 2073 protein complexes with less than 90% sequence identity - out of the protein database, which can serve as bi- or multivalent receptors. Steric clashes of molecular spacers - necessary to connect the monomeric ligand units - with the receptor surface can diminish binding affinity dramatically and, thus, abolish the expected enhancement of binding affinity due to the multivalency. The potential multivalent receptors in the Bival-Bind database are characterized with respect to the receptor surface topography. A height profile between the receptor binding pockets is provided, which is an important information to estimate the influence of unfavorable spacer receptor interaction. |