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Titolo:
STRUCTURAL MOTIFS AT PROTEIN-PROTEIN INTERFACES - PROTEIN CORES VERSUS 2-STATE AND 3-STATE MODEL COMPLEXES
Autore:
TSAI CJ; XU D; NUSSINOV R;
Indirizzi:
NCI,FREDERICK CANC RES & DEV CTR,MATH BIOL LAB,SAIC,BLDG 469,ROOM 151FREDERICK MD 21702 NCI,FREDERICK CANC RES & DEV CTR,MATH BIOL LAB,SAIC FREDERICK MD 21702 TEL AVIV UNIV,SACKLER INST MOL MED IL-69978 TEL AVIV ISRAEL
Titolo Testata:
Protein science
fascicolo: 9, volume: 6, anno: 1997,
pagine: 1793 - 1805
SICI:
0961-8368(1997)6:9<1793:SMAPI->2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLOBULAR-PROTEINS; SUBUNIT INTERFACES; FOLD FAMILIES; DATA-BANK; CLASSIFICATION; SEQUENCES; IDENTIFICATION; SIMILARITIES; RECOGNITION; DYNAMICS;
Keywords:
HYDROPHOBIC EFFECT; MOTIFS; PROTEIN FOLDING; PROTEIN-PROTEIN INTERFACES; PROTEIN-PROTEIN RECOGNITION; STRUCTURAL COMPARISON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
C.J. Tsai et al., "STRUCTURAL MOTIFS AT PROTEIN-PROTEIN INTERFACES - PROTEIN CORES VERSUS 2-STATE AND 3-STATE MODEL COMPLEXES", Protein science, 6(9), 1997, pp. 1793-1805

Abstract

The general similarity in the forces governing protein folding and protein-protein associations has led us to examine the similarity in thearchitectural motifs between the interfaces and the monomers. We havecarried out extensive, all-against-all structural comparisons betweenthe single-chain protein structural dataset and the interface dataset, derived both from all protein-protein complexes in the structural database and from interfaces generated via an automated crystal symmetryoperation. We show that despite the absence of chain connections, theglobal features of the architectural motifs, present in monomers, recur in the interfaces, a reflection of the limited set of the folding patterns. However, although similarity has been observed, the details of the architectural motifs vary. In particular, the extent of the similarity correlates with the consideration of how the interface has beenformed. Interfaces derived from two-state model complexes, where the chains fold cooperatively, display a considerable similarity to architectures in protein cores, as judged by the quality of their geometric superposition. On the other hand, the three-state model interfaces, representing binding of already folded molecules, manifest a larger variability and resemble the monomer architecture only in general outline. The origin of the difference between the monomers and the three-statemodel interfaces can be understood in terms of the different nature of the folding and the binding that are involved. Whereas in the formerall degrees of freedom are available to the backbone to maximize favorable interactions, in rigid body, three-state model binding, only sixdegrees of freedom are allowed. Hence, residue or atom pair-wise potentials derived from protein-protein associations are expected to be less accurate, substantially increasing the number of computationally acceptable alternate binding modes (Finkelstein et al., 1995).

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Documento generato il 29/11/20 alle ore 03:33:51