Intrinsic protein disorder and protein-protein interactions.

Wei Lun Hsu, Christopher Oldfield, Jingwei Meng, Fei Huang, Bin Xue, Vladimir N. Uversky, Pedro Romero, A. Dunker

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity at structurally aligned positions. As it turned out that most of the examples so selected had similar 3D structure, the studied set was reduced to just these similar-fold cases. Based on the analyses of the interacting partners, the average sequence identity of the partners' binding regions showed substantially higher conservation as compared to the nonbinding regions: The residue identities, averaged over the 11 sets of partner proteins, were as follows: binding residues, 42 ± 6%; nonbinding residues 20 ± 3%; nonbinding buried residues 26 ± 5%; and nonbinding surface residues 16 ± 3%. The higher sequence identity of the binding residues compared to the other sets of residues provides evidence that these observed interactions are likely to be meaningful biological interactions, not artifacts. Since many of the features of the various interactions indicate that the disordered binding segments were likely to have been disordered before binding, these results also add further weight to the existence and function of intrinsically disordered regions inside cells.

Original languageEnglish (US)
Pages (from-to)116-127
Number of pages12
JournalPacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
StatePublished - 2012

Fingerprint

Intrinsically Disordered Proteins
Artifacts
Proteins
Amino Acids
Weights and Measures

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Intrinsic protein disorder and protein-protein interactions. / Hsu, Wei Lun; Oldfield, Christopher; Meng, Jingwei; Huang, Fei; Xue, Bin; Uversky, Vladimir N.; Romero, Pedro; Dunker, A.

In: Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing, 2012, p. 116-127.

Research output: Contribution to journalArticle

Hsu, WL, Oldfield, C, Meng, J, Huang, F, Xue, B, Uversky, VN, Romero, P & Dunker, A 2012, 'Intrinsic protein disorder and protein-protein interactions.', Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing, pp. 116-127.
Hsu, Wei Lun ; Oldfield, Christopher ; Meng, Jingwei ; Huang, Fei ; Xue, Bin ; Uversky, Vladimir N. ; Romero, Pedro ; Dunker, A. / Intrinsic protein disorder and protein-protein interactions. In: Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing. 2012 ; pp. 116-127.
@article{a026d51e5c3a4c10bac7b450f46cea63,
title = "Intrinsic protein disorder and protein-protein interactions.",
abstract = "Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25{\%} amino acid identity at structurally aligned positions. As it turned out that most of the examples so selected had similar 3D structure, the studied set was reduced to just these similar-fold cases. Based on the analyses of the interacting partners, the average sequence identity of the partners' binding regions showed substantially higher conservation as compared to the nonbinding regions: The residue identities, averaged over the 11 sets of partner proteins, were as follows: binding residues, 42 ± 6{\%}; nonbinding residues 20 ± 3{\%}; nonbinding buried residues 26 ± 5{\%}; and nonbinding surface residues 16 ± 3{\%}. The higher sequence identity of the binding residues compared to the other sets of residues provides evidence that these observed interactions are likely to be meaningful biological interactions, not artifacts. Since many of the features of the various interactions indicate that the disordered binding segments were likely to have been disordered before binding, these results also add further weight to the existence and function of intrinsically disordered regions inside cells.",
author = "Hsu, {Wei Lun} and Christopher Oldfield and Jingwei Meng and Fei Huang and Bin Xue and Uversky, {Vladimir N.} and Pedro Romero and A. Dunker",
year = "2012",
language = "English (US)",
pages = "116--127",
journal = "Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing",
issn = "2335-6936",

}

TY - JOUR

T1 - Intrinsic protein disorder and protein-protein interactions.

AU - Hsu, Wei Lun

AU - Oldfield, Christopher

AU - Meng, Jingwei

AU - Huang, Fei

AU - Xue, Bin

AU - Uversky, Vladimir N.

AU - Romero, Pedro

AU - Dunker, A.

PY - 2012

Y1 - 2012

N2 - Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity at structurally aligned positions. As it turned out that most of the examples so selected had similar 3D structure, the studied set was reduced to just these similar-fold cases. Based on the analyses of the interacting partners, the average sequence identity of the partners' binding regions showed substantially higher conservation as compared to the nonbinding regions: The residue identities, averaged over the 11 sets of partner proteins, were as follows: binding residues, 42 ± 6%; nonbinding residues 20 ± 3%; nonbinding buried residues 26 ± 5%; and nonbinding surface residues 16 ± 3%. The higher sequence identity of the binding residues compared to the other sets of residues provides evidence that these observed interactions are likely to be meaningful biological interactions, not artifacts. Since many of the features of the various interactions indicate that the disordered binding segments were likely to have been disordered before binding, these results also add further weight to the existence and function of intrinsically disordered regions inside cells.

AB - Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity at structurally aligned positions. As it turned out that most of the examples so selected had similar 3D structure, the studied set was reduced to just these similar-fold cases. Based on the analyses of the interacting partners, the average sequence identity of the partners' binding regions showed substantially higher conservation as compared to the nonbinding regions: The residue identities, averaged over the 11 sets of partner proteins, were as follows: binding residues, 42 ± 6%; nonbinding residues 20 ± 3%; nonbinding buried residues 26 ± 5%; and nonbinding surface residues 16 ± 3%. The higher sequence identity of the binding residues compared to the other sets of residues provides evidence that these observed interactions are likely to be meaningful biological interactions, not artifacts. Since many of the features of the various interactions indicate that the disordered binding segments were likely to have been disordered before binding, these results also add further weight to the existence and function of intrinsically disordered regions inside cells.

UR - http://www.scopus.com/inward/record.url?scp=84891387199&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84891387199&partnerID=8YFLogxK

M3 - Article

C2 - 22174268

AN - SCOPUS:84891387199

SP - 116

EP - 127

JO - Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing

JF - Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing

SN - 2335-6936

ER -