A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein
Identifying hot-spot residues – residues that are critical to protein–protein binding – can help to elucidate a protein's function and assist in designing therapeutic molecules to target those residues. We present a novel computational tool, termed spatial-interaction-map (SIM), to predict the...
| Main Authors: | , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
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Elsevier
2016
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| Online Access: | http://hdl.handle.net/1721.1/101385 https://orcid.org/0000-0003-1417-9470 |
| _version_ | 1826211472712138752 |
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| author | Agrawal, Neeraj J. Helk, Bernhard Trout, Bernhardt L. |
| author2 | Massachusetts Institute of Technology. Department of Chemical Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Chemical Engineering Agrawal, Neeraj J. Helk, Bernhard Trout, Bernhardt L. |
| author_sort | Agrawal, Neeraj J. |
| collection | MIT |
| description | Identifying hot-spot residues – residues that are critical to protein–protein binding – can help to elucidate a protein's function and assist in designing therapeutic molecules to target those residues. We present a novel computational tool, termed spatial-interaction-map (SIM), to predict the hot-spot residues of an evolutionarily conserved protein–protein interaction from the structure of an unbound protein alone. SIM can predict the protein hot-spot residues with an accuracy of 36–57%. Thus, the SIM tool can be used to predict the yet unknown hot-spot residues for many proteins for which the structure of the protein–protein complexes are not available, thereby providing a clue to their functions and an opportunity to design therapeutic molecules to target these proteins. |
| first_indexed | 2024-09-23T15:06:26Z |
| format | Article |
| id | mit-1721.1/101385 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T15:06:26Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/1013852022-09-29T12:44:50Z A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein Agrawal, Neeraj J. Helk, Bernhard Trout, Bernhardt L. Massachusetts Institute of Technology. Department of Chemical Engineering Trout, Bernhardt L. Agrawal, Neeraj J. Trout, Bernhardt L. Identifying hot-spot residues – residues that are critical to protein–protein binding – can help to elucidate a protein's function and assist in designing therapeutic molecules to target those residues. We present a novel computational tool, termed spatial-interaction-map (SIM), to predict the hot-spot residues of an evolutionarily conserved protein–protein interaction from the structure of an unbound protein alone. SIM can predict the protein hot-spot residues with an accuracy of 36–57%. Thus, the SIM tool can be used to predict the yet unknown hot-spot residues for many proteins for which the structure of the protein–protein complexes are not available, thereby providing a clue to their functions and an opportunity to design therapeutic molecules to target these proteins. Novartis (Firm) Singapore-MIT Alliance for Research and Technology 2016-03-01T20:12:23Z 2016-03-01T20:12:23Z 2013-11 2013-11 Article http://purl.org/eprint/type/JournalArticle 00145793 1873-3468 http://hdl.handle.net/1721.1/101385 Agrawal, Neeraj J., Bernhard Helk, and Bernhardt L. Trout. “A Computational Tool to Predict the Evolutionarily Conserved Protein-Protein Interaction Hot-Spot Residues from the Structure of the Unbound Protein.” FEBS Letters 588, no. 2 (November 12, 2013): 326–333. https://orcid.org/0000-0003-1417-9470 en_US http://dx.doi.org/10.1016/j.febslet.2013.11.004 FEBS Letters Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier Prof. Trout via Erja Kajosalo |
| spellingShingle | Agrawal, Neeraj J. Helk, Bernhard Trout, Bernhardt L. A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title | A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title_full | A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title_fullStr | A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title_full_unstemmed | A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title_short | A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein |
| title_sort | computational tool to predict the evolutionarily conserved protein protein interaction hot spot residues from the structure of the unbound protein |
| url | http://hdl.handle.net/1721.1/101385 https://orcid.org/0000-0003-1417-9470 |
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