α-Helical Protein Assembly Motifs

Kohn, Wayne D.; Mant, Colin T.; Hodges, Robert S.

doi:10.1074/jbc.272.5.2583

Cited by 185 publications

(138 citation statements)

References 118 publications

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“…1) residues, which due to their charged side chains are also likely to interact in intermolecular complexes. This reggie/flotillin arrangement fits well with the typical requirements for the formation of coiled-coil-based oligomeric complexes [35], which are probably the most common oligomerization motif found in proteins [53]. Moreover, reggie/flotillin tandem heptad arrays are organized in three clusters disrupted by incomplete heptads, creating the potential for each of them to interact independently with a different partner molecule ( fig.…”

Section: Discussionsupporting

confidence: 76%

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

Rivera-Milla

Stuermer

Málaga-Trillo

2006

Cell. Mol. Life Sci.

145

150

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Abstract. Reggies (flotillins) are detergent-resistant microdomains involved in the scaffolding of large heteromeric complexes that signal across the plasma membrane. Based on the presence of an evolutionarily widespread motif, reggies/flotillins have been included within the SPFH (stomatin-prohibitin-flotillin-HflC/K) protein superfamily. To better understand the origin and evolution of reggie/flotillin structure and function, we searched databases for reggie/flotillin and SPFH-like proteins in organisms at the base and beyond the animal kingdom, and used the resulting dataset to compare their structural Cell. Mol. Life Sci. 63 (2006) 343-357 1420-682X/06/030343-15 DOI 10.1007/s00018-005-5434-3 © Birkhäuser Verlag, Basel, 2006 and functional domains. Our analysis shows that the SPFH grouping has little phylogenetic support, probably due to convergent evolution of its members. We also find that reggie/flotillin homologues are highly conserved among metazoans but are absent in plants, fungi and bacteria, where only proteins with 'reggie-like' domains can be found. However, despite their low sequence similarities, reggie/flotillin and 'reggie-like' domains appear to subserve related functions, suggesting that their basic biological role was acquired independently during evolution.

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Section: Discussionsupporting

confidence: 76%

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

Rivera-Milla

Stuermer

Málaga-Trillo

2006

Cell. Mol. Life Sci.

145

150

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“…20 The spectrum also shows a small induced CD band in the Soret region of the spectrum consisting of a negative peak at 420 nm and maximum at 434 nm.…”

Section: Resultsmentioning

confidence: 99%

Self-Organization of porphyrin-peptide units by metal-mediated peptide assembly

Carvalho¹,

Ogawa²

2010

J. Braz. Chem. Soc.

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O polipeptídeo H21(30-mer) forma dímeros "coiled-coil" que apresentam dois resíduos histidínicos expostos ao solvente nos lados opostos de sua superfície. Este peptídeo reage com a protoporfirina IX de cobalto, Co(ppIX), para produzir [Co(ppIX){(H21(30-mer)} 2 ], como determinado por espectroscopia UV-Vis. Esta ligação bi-axial disponibiliza um potencial domínio de oligomerização "coiled-coil" em cada face do anel porfirínico de cobalto. Dicroísmo circular e cromatografia líquida de exclusão de alto desempenho forneceram evidências da auto-organização destas unidades porfirina-peptídeo em solução. A evaporação da solução porfirina-peptídeo em uma superfície sólida resultou na formação de longos materiais cilíndricos com milímetros de comprimento e micrometros de diâmetro. A presença do complexo Co(ppIX) nestes materiais foi confirmada por microscopia Raman. Estes materiais, entretanto, foram formados somente com o tampão fosfato, e não com tampões orgânicos ou água pura, indicando que sua formação deve envolver um processo mais complicado do que originalmente antecipado.The polypeptide H21(30-mer) folds into a two-stranded coiled-coil in which two solventexposed histidine residues reside on opposite sides of its surface. This peptide was allowed to react with cobalt(III) protoporphyrin IX, Co(ppIX), to produce [Co(ppIX){(H21(30-mer)} 2 ], as determined by UV-Vis spectroscopy. This bis-axial ligation thus positions a potential coiledcoil oligomerization domain onto each face of the cobalt porphyrin ring. Circular dichroism spectroscopy and high performance size exclusion chromatography provide evidence for the solution-phase self-assembly of these porphyrin-peptide units. Evaporation of the porphyrinpeptide solution on a solid support results in the formation of long rod-like materials having millimeter-scale lengths and micron-scale diameters. The presence of Co(ppIX) in these materials was confirmed by Raman microscopy. However, they were formed only from phosphate buffer, and not from organic buffers or pure water, indicating that their formation might involve a more complicated process than originally anticipated.Keywords: cobalt protoporphyrin IX, peptides, fibers, self-assembly IntroductionMolecular self-assembly has proven to be a valuable approach towards the bottom-up design of synthetic materials. [1][2][3][4][5] Much inspiration for this work comes from biological precedents in which optimal combinations of hydrogen-bond, electrostatic, and hydrophobic interactions are used to assemble polypeptides and nucleic acids into robust structural motifs. 2,4 To further expand the tools for preparing such materials, continuing efforts are being directed towards gaining a better understanding of how various combination of non-covalent interactions can be used to prepare self-assembled materials having predictable and well-defined morphologies. 6,7 Inspired by workers in the field of supramolecular coordination chemistry, we 8-12 and others [13][14][15][16] have been exploring a new route for preparing self-assem...

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“…Each segment therefore only contained three collagenous triplets at its N-terminal end, out of the 26-27 repeats in the fulllength A, B, and C chains. Since, formation of a collagen-like triple helix requires multiple collagenous repeats, the three repeats left after collagenase treatment were unlikely to be sufficient for the generation of a triple helix and trimerization of the C-terminal domain [16].…”

Section: Resultsmentioning

confidence: 99%

Trimeric reassembly of the globular domain of human C1q

Tacnet

Cheong

Goeltz

et al. 2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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C1q is a versatile recognition protein which binds to a variety of targets and consequently triggers the classical pathway of complement. C1q is a hetero-trimer composed of three chains (A, B and C) arranged in three domains, a short N-terminal region, followed by a collagenous repeat domain that gives rise to the formation of (ABC) triple helices, each ending in a C-terminal hetero-trimeric globular domain, called gC1q, which is responsible for the recognition properties of C1q. The mechanism of the trimeric assembly of C1q and in particular the role of each domain in the process is unknown. Here, we have investigated if the gC1q domain was able to assemble into functional trimers, in vitro, in the absence of the collagenous domain, a motif known to promote obligatory trimers in other proteins. Acid-mediated gC1q protomers reassembled into functional trimers, once neutralized, indicating that it is the gC1q domain which possesses the information for trimerization. However, reassembly occurred after neutralization, only if the gC1q protomers had preserved a residual tertiary structure at the end of the acidic treatment. Thus, the collagenous domain of C1q might initialize the folding of the gC1q domain so that subsequent assembly of the entire molecule can occur.

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α-Helical Protein Assembly Motifs

Cited by 185 publications

References 118 publications

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain

Self-Organization of porphyrin-peptide units by metal-mediated peptide assembly

Trimeric reassembly of the globular domain of human C1q

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