FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2013988051> ?p ?o ?g. }

• W2013988051 endingPage "342" @default.
• W2013988051 startingPage "331" @default.
• W2013988051 abstract "A number of studies have addressed the question of which are the critical residues at protein-binding sites. These studies examined either a single or a few protein–protein interfaces. The most extensive study to date has been an analysis of alanine-scanning mutagenesis. However, although the total number of mutations was large, the number of protein interfaces was small, with some of the interfaces closely related. Here we show that although overall binding sites are hydrophobic, they are studded with specific, conserved polar residues at specific locations, possibly serving as energy “hot spots.” Our results confirm and generalize the alanine-scanning data analysis, despite its limited size. Previously Trp, Arg, and Tyr were shown to constitute energetic hot spots. These were rationalized by their polar interactions and by their surrounding rings of hydrophobic residues. However, there was no compelling reason as to why specifically these residues were conserved. Here we show that other polar residues are similarly conserved. These conserved residues have been detected consistently in all interface families that we have examined. Our results are based on an extensive examination of residues which are in contact across protein interfaces. We utilize all clustered interface families with at least five members and with sequence similarity between the members in the range of 20–90%. There are 11 such clustered interface families, comprising a total of 97 crystal structures. Our three-dimensional superpositioning analysis of the occurrences of matched residues in each of the families identifies conserved residues at spatially similar environments. Additionally, in enzyme inhibitors, we observe that residues are more conserved at the interfaces than at other locations. On the other hand, antibody–protein interfaces have similar surface conservation as compared to their corresponding linear sequence alignment, consistent with the suggestion that evolution has optimized protein interfaces for function. Proteins 2000;39:331–342. © 2000 Wiley-Liss, Inc." @default.
• W2013988051 created "2016-06-24" @default.
• W2013988051 creator A5025357844 @default.
• W2013988051 creator A5030975599 @default.
• W2013988051 creator A5068900909 @default.
• W2013988051 creator A5076498226 @default.
• W2013988051 date "2000-06-01" @default.
• W2013988051 modified "2023-10-07" @default.
• W2013988051 title "Conservation of polar residues as hot spots at protein interfaces" @default.
• W2013988051 cites W1490071206 @default.
• W2013988051 cites W1524608481 @default.
• W2013988051 cites W1596369886 @default.
• W2013988051 cites W1625079248 @default.
• W2013988051 cites W1965907701 @default.
• W2013988051 cites W1966041739 @default.
• W2013988051 cites W1971187927 @default.
• W2013988051 cites W1980353405 @default.
• W2013988051 cites W1983036219 @default.
• W2013988051 cites W1984218254 @default.
• W2013988051 cites W1992558926 @default.
• W2013988051 cites W1997814593 @default.
• W2013988051 cites W1998645872 @default.
• W2013988051 cites W2000980755 @default.
• W2013988051 cites W2008421309 @default.
• W2013988051 cites W2010122910 @default.
• W2013988051 cites W2011845231 @default.
• W2013988051 cites W2021411698 @default.
• W2013988051 cites W2023048070 @default.
• W2013988051 cites W2031772330 @default.
• W2013988051 cites W2036835637 @default.
• W2013988051 cites W2040159113 @default.
• W2013988051 cites W2048639821 @default.
• W2013988051 cites W2048792959 @default.
• W2013988051 cites W2051710717 @default.
• W2013988051 cites W2058527555 @default.
• W2013988051 cites W2075770210 @default.
• W2013988051 cites W2086429541 @default.
• W2013988051 cites W2086635082 @default.
• W2013988051 cites W2089088187 @default.
• W2013988051 cites W2094090446 @default.
• W2013988051 cites W2101362041 @default.
• W2013988051 cites W2113030357 @default.
• W2013988051 cites W2123529526 @default.
• W2013988051 cites W2124013748 @default.
• W2013988051 cites W2132709044 @default.
• W2013988051 cites W2147274570 @default.
• W2013988051 cites W2158919479 @default.
• W2013988051 cites W2164460047 @default.
• W2013988051 cites W2165214884 @default.
• W2013988051 cites W4248357178 @default.
• W2013988051 doi "https://doi.org/10.1002/(sici)1097-0134(20000601)39:4<331::aid-prot60>3.0.co;2-a" @default.
• W2013988051 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10813815" @default.
• W2013988051 hasPublicationYear "2000" @default.
• W2013988051 type Work @default.
• W2013988051 sameAs 2013988051 @default.
• W2013988051 citedByCount "271" @default.
• W2013988051 countsByYear W20139880512012 @default.
• W2013988051 countsByYear W20139880512013 @default.
• W2013988051 countsByYear W20139880512014 @default.
• W2013988051 countsByYear W20139880512015 @default.
• W2013988051 countsByYear W20139880512016 @default.
• W2013988051 countsByYear W20139880512017 @default.
• W2013988051 countsByYear W20139880512018 @default.
• W2013988051 countsByYear W20139880512019 @default.
• W2013988051 countsByYear W20139880512020 @default.
• W2013988051 countsByYear W20139880512021 @default.
• W2013988051 countsByYear W20139880512022 @default.
• W2013988051 countsByYear W20139880512023 @default.
• W2013988051 crossrefType "journal-article" @default.
• W2013988051 hasAuthorship W2013988051A5025357844 @default.
• W2013988051 hasAuthorship W2013988051A5030975599 @default.
• W2013988051 hasAuthorship W2013988051A5068900909 @default.
• W2013988051 hasAuthorship W2013988051A5076498226 @default.
• W2013988051 hasConcept C104317684 @default.
• W2013988051 hasConcept C11804247 @default.
• W2013988051 hasConcept C121332964 @default.
• W2013988051 hasConcept C12554922 @default.
• W2013988051 hasConcept C1276947 @default.
• W2013988051 hasConcept C16318435 @default.
• W2013988051 hasConcept C167625842 @default.
• W2013988051 hasConcept C185592680 @default.
• W2013988051 hasConcept C199216141 @default.
• W2013988051 hasConcept C2779856020 @default.
• W2013988051 hasConcept C2780227090 @default.
• W2013988051 hasConcept C29705727 @default.
• W2013988051 hasConcept C47701112 @default.
• W2013988051 hasConcept C501734568 @default.
• W2013988051 hasConcept C515207424 @default.
• W2013988051 hasConcept C55493867 @default.
• W2013988051 hasConcept C8010536 @default.
• W2013988051 hasConcept C86803240 @default.
• W2013988051 hasConceptScore W2013988051C104317684 @default.
• W2013988051 hasConceptScore W2013988051C11804247 @default.
• W2013988051 hasConceptScore W2013988051C121332964 @default.
• W2013988051 hasConceptScore W2013988051C12554922 @default.
• W2013988051 hasConceptScore W2013988051C1276947 @default.
• W2013988051 hasConceptScore W2013988051C16318435 @default.
• W2013988051 hasConceptScore W2013988051C167625842 @default.

• next