2008
DOI: 10.1073/pnas.0709068105
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Preferred side-chain constellations at antiparallel coiled-coil interfaces

Abstract: Reliable predictive rules that relate protein sequence to structure would facilitate postgenome predictive biology and the engineering and de novo design of peptides and proteins. Through a combination of experiment and analysis of the protein data bank (PDB), we have deciphered and rationalized new rules for helixhelix interfaces of a common protein-folding and association motif, the antiparallel dimeric coiled coil. These interfaces are defined by a specific pattern of interactions among largely hydrophobic … Show more

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Cited by 76 publications
(107 citation statements)
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References 42 publications
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“…Another study is now underway to identify whether the two proteins, NSrp70 and pumilio, have any functional similarity. Proteins containing the CC domain are known to induce homophilic oligomerization through dimeric or trimetric interactions (40,41). Consistent with this, we found that NSrp70 could self-interact to form multimers through the CC domain and that multimerization influenced its alternative splicing activity but had no effect on binding to SR proteins or to target mRNA.…”
Section: Discussionsupporting
confidence: 72%
“…Another study is now underway to identify whether the two proteins, NSrp70 and pumilio, have any functional similarity. Proteins containing the CC domain are known to induce homophilic oligomerization through dimeric or trimetric interactions (40,41). Consistent with this, we found that NSrp70 could self-interact to form multimers through the CC domain and that multimerization influenced its alternative splicing activity but had no effect on binding to SR proteins or to target mRNA.…”
Section: Discussionsupporting
confidence: 72%
“…Anti-parallel coiled-coils form sequential intermolecular interactions between branched hydrophobic residues at a and a as well as d and d positions of the heptad repeat in the two chains. Recent work indicates that select triplet repeats at the a-a-a positions favor heterodimeric coiled-coil formation, with LIL or ILI triplets the most favored combination (27). As can be seen in Fig.…”
Section: Conservation Of Hydrophobic Interactions-mentioning
confidence: 50%
“…[38][39][40] The knobs-into-holes packing of ''b-e'' and ''c-g'' interfaces for a 4 F 3 a and a 4 F 3 d contain only like residues, in which Leu residues pack exclusively into the vertical hole created by two Leu residues of the adjacent helix and hFLeu residues follow a similar packing arrangement at the opposite interface. This creates a very regular packing arrangement.…”
Section: Discussionmentioning
confidence: 99%