Principles of Protein-Protein Interactions
This review examines protein complexes in the Brookhaven Protein Databank to gain a better understanding of the principles governing the interactions involved in protein-protein recognition. The factors that influence the formation of protein-protein complexes are explored in four different types of...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-01, Vol.93 (1), p.13-20 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Jones, Susan Thornton, Janet M. |
description | This review examines protein complexes in the Brookhaven Protein Databank to gain a better understanding of the principles governing the interactions involved in protein-protein recognition. The factors that influence the formation of protein-protein complexes are explored in four different types of protein-protein complexes--homodimeric proteins, heterodimeric proteins, enzyme-inhibitor complexes, and antibody-protein complexes. The comparison between the complexes highlights differences that reflect their biological roles. |
doi_str_mv | 10.1073/pnas.93.1.13 |
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The comparison between the complexes highlights differences that reflect their biological roles.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.1.13</identifier><identifier>PMID: 8552589</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino acids ; Animals ; Antigen-Antibody Complex - chemistry ; Atoms ; Crystallography, X-Ray ; Cytochromes ; Datasets ; Dimers ; Humans ; Hydrogen Bonding ; Hydrogen bonds ; Hydrophobicity ; Macromolecular Substances ; Molecular biology ; Molecular weight ; Molecules ; Monomers ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Proteins ; Proteins - chemistry ; Review ; Solubility ; Structure-Activity Relationship</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-01, Vol.93 (1), p.13-20</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Jan 9, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-6b911244657baa7e190a2a1f5b3b1216967e1fd3698fcb2ba2ce993a2a57c8383</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/38302$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/38302$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27923,27924,53790,53792,58016,58249</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8552589$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jones, Susan</creatorcontrib><creatorcontrib>Thornton, Janet M.</creatorcontrib><title>Principles of Protein-Protein Interactions</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>This review examines protein complexes in the Brookhaven Protein Databank to gain a better understanding of the principles governing the interactions involved in protein-protein recognition. The factors that influence the formation of protein-protein complexes are explored in four different types of protein-protein complexes--homodimeric proteins, heterodimeric proteins, enzyme-inhibitor complexes, and antibody-protein complexes. The comparison between the complexes highlights differences that reflect their biological roles.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Antigen-Antibody Complex - chemistry</subject><subject>Atoms</subject><subject>Crystallography, X-Ray</subject><subject>Cytochromes</subject><subject>Datasets</subject><subject>Dimers</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Hydrophobicity</subject><subject>Macromolecular Substances</subject><subject>Molecular biology</subject><subject>Molecular weight</subject><subject>Molecules</subject><subject>Monomers</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Review</subject><subject>Solubility</subject><subject>Structure-Activity Relationship</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFLHDEUh4O06Gq9ebIUFhEP4qx5SSaTgBdZ1C4I9dCeQyZm7CyzyZpkpP73zbDjYgulpwf5vt_jvTyEjgDPAFf0cu10nEk6gxnQHTQBLKHgTOIPaIIxqQrBCNtD-zEuMcayFHgX7YqyJKWQE3T-EFpn2nVn49Q304fgk21dMdbpwiUbtEmtd_ET-tjoLtrDsR6gH7c33-dfi_tvd4v59X1hSsZTwWsJQBjjZVVrXVmQWBMNTVnTGghwyfNb80i5FI2pSa2JsVLS7JSVEVTQA3S16bvu65V9NNaloDu1Du1Kh1fldav-JK79qZ78i2IYKpzjZ2M8-OfexqRWbTS267Szvo-qqiTnjPxfzM1E7jcMdPKXuPR9cPkPFMHACAjBs3SxkUzwMQbbbAcGrIY7qeFOSlIFCmjWv7xfciuPh8n8dORD6o2OadX0XZfsr5S1z__WMj3e0GVMPmxxXgkT-hs5u61K</recordid><startdate>19960109</startdate><enddate>19960109</enddate><creator>Jones, Susan</creator><creator>Thornton, Janet M.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19960109</creationdate><title>Principles of Protein-Protein Interactions</title><author>Jones, Susan ; Thornton, Janet M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546t-6b911244657baa7e190a2a1f5b3b1216967e1fd3698fcb2ba2ce993a2a57c8383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Antigen-Antibody Complex - chemistry</topic><topic>Atoms</topic><topic>Crystallography, X-Ray</topic><topic>Cytochromes</topic><topic>Datasets</topic><topic>Dimers</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Hydrophobicity</topic><topic>Macromolecular Substances</topic><topic>Molecular biology</topic><topic>Molecular weight</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Review</topic><topic>Solubility</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jones, Susan</creatorcontrib><creatorcontrib>Thornton, Janet M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jones, Susan</au><au>Thornton, Janet M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Principles of Protein-Protein Interactions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-01-09</date><risdate>1996</risdate><volume>93</volume><issue>1</issue><spage>13</spage><epage>20</epage><pages>13-20</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>This review examines protein complexes in the Brookhaven Protein Databank to gain a better understanding of the principles governing the interactions involved in protein-protein recognition. 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subjects | Amino acids Animals Antigen-Antibody Complex - chemistry Atoms Crystallography, X-Ray Cytochromes Datasets Dimers Humans Hydrogen Bonding Hydrogen bonds Hydrophobicity Macromolecular Substances Molecular biology Molecular weight Molecules Monomers Protein Binding Protein Conformation Protein Structure, Secondary Proteins Proteins - chemistry Review Solubility Structure-Activity Relationship |
title | Principles of Protein-Protein Interactions |
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