Quaternary Structure of Proteins

Klotz, Irving M.; Darnall, Dennis W.; Langerman, Neal

doi:10.1016/b978-0-12-516301-9.50009-7

Cited by 100 publications

(77 citation statements)

References 319 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Pentameric structures are relatively rare configurations for proteins [50]. Theoretically, the monomers in an oligomeric macromolecule could be assembled in a variety of different geometries that depend on the saturation of the interface bonding potentials and the environment of each of the monomers.…”

Section: Discussionmentioning

confidence: 99%

“…Theoretically, the monomers in an oligomeric macromolecule could be assembled in a variety of different geometries that depend on the saturation of the interface bonding potentials and the environment of each of the monomers. If each of the monomers of the oligomer is in an identical environment and if the bonding potential of the monomers is saturated, then the only possible arrangement of a pentamer is cyclic symmetry [50], with the monomers arranged at the corners of a pentagon. Indeed, the structure of the rabbit CRP shows a cyclic pentamer.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Two‐dimensional crystallization of rabbit C‐reactive protein on lipid monolayers

Sui

Liu

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Two‐dimensional crystallization of rabbit C‐reactive protein on lipid monolayers

Sui

Liu

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

“…Pentameric structures are relatively rare configurations for proteins (28). Theoretically, the protomers in an oligomeric macromolecule could be arranged in a variety of different geometries that depend on the saturation of the interface bonding potentials and the environment of each of the pro- Table 2).…”

Section: Resultsmentioning

confidence: 99%

Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins).

Osmand¹,

Friedenson²,

Gewürz³

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

316

145

View full text Add to dashboard Cite

Partial amino acid sequences of rabbit C-reactive protein, a peptide derived from human C-reactive protein by cyanogen bromide cleavage, and the Cit subcomponent of the human complement component CI have been determined. Extensive sequence homology between these proteins establish their evolutionary relationships. In addition, examination of C-reactive proteins by negative-stain electron microscopy revealed that the protein is composed of five subunits arranged in cyclic symmetry. This structure is similar to that reported for both Cit and the amyloid P-component. The extensive structural relationship suggests similar or overlapping functions and the term pentraxin is proposed to describe these homologous proteins.Activation of the primary complement (C) pathway is one of the principle biological activities of immunoglobulins. The C pathway sequence is initiated via an interaction between the Fc region of certain immunoglobulins and the C1 macromolecular complex, which leads to an internal activation of C1 and the generation of its proteolytic activity (1). During recent years several alternative mechanisms for the activation of the C system have been described. Most of these activators operate through one or another of the complex maze of interactions known as the properdin or alternative pathway (2). However, one of these agents, C-reactive protein (CRP), would appear to act in a manner entirely analogous to immunoglobulin. It has been found that upon interaction with a variety of substances, CRP can activate the C cascade and initiate both the opsonic and lytic potentials of this system through an activation of the primary C pathway (3-6). CRP has been described as being comprised of probably identical subunits, ca 23,000 daltons, noncovalently linked to form an oligomer of molecular weight 120,000-140,000 (7,8 During preliminary presentations (15, 16) of some of the data described here, an extensive amino acid-sequence homology (ca 50%) between CRP and Cit was noted. Although there are no a priori reasons to preclude such an extensive homology between an activator of C1 and one of its subcomponents, this was unexpected. We report here partial amino acid sequences of human and rabbit CRP and human Cit that establish the evolutionary relatedness of these proteins. In addition, we present a detailed ultrastructural analysis of both human and rabbit CRP by negative stain electron microscopy that shows it to be assembled as a cyclic pentamer, in a manner similar to both Cit and amyloid P-component. The term pentraxin (Greek. revrE, five and 'pat, berry) is proposed to describe these related proteins.MATERIALS AND METHODS C-Reactive Proteins. Human CRP was isolated by affinity chromatography of human serous fluids on agarose beads (Bio-Gel A-15m) to which pneumococcal C-polysaccharide was covalently linked (5). Subunits and aggregates of CRP were removed from the native protein by gel filtration in Trisbuffered saline on Bio-Gel A-0.5m. The purity of such preparations of CRP has been previously established...

show abstract

“…For a tetramer, if only closed [22], nonmixed [23] structures are considered of all arrangements, the following possibilities exist.…”

Section: Theoretical Prediction Of Crosslinking Patterns For Tetramermentioning

confidence: 99%

Crosslinking with Bifunctional Reagents as a Means for Studying the Symmetry of Oligomeric Proteins

Hajdu

Bartha

Friedrich

1976

European Journal of Biochemistry

View full text Add to dashboard Cite

A method based upon the principle that unlike domains of bonding are reflected in different re‐activities and distribution of residues that can be crosslinked, has been elaborated for the determination of symmetry of oligomeric proteins. The derivation of theoretical curves for the prediction of crosslinking patterns of tetramers produced by reaction with a bifunctional reagent and subsequent sodium‐dodecylsulphate‐gel electrophoretic analysis is presented. Based upon the theory the symmetry properties of a tetramer, to the extent whether it is an isologous or heterologous associationn, can be deduced by a simple calculation. Crosslinking patterns obtained with rabbit muscle aldolase and pig muscle lactate dehydrogenase after treatment with a series of diimidoesters of increasing chain length are evaluated and shown to be consistent with the expectations for isologous tetramers. From the patterns obtained with the various reagents the distances between lysyl residues located nearest to each other in different subunits in the two proteins could also be determined.

show abstract

Quaternary Structure of Proteins

Cited by 100 publications

References 319 publications

Two‐dimensional crystallization of rabbit C‐reactive protein on lipid monolayers

Two‐dimensional crystallization of rabbit C‐reactive protein on lipid monolayers

Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins).

Crosslinking with Bifunctional Reagents as a Means for Studying the Symmetry of Oligomeric Proteins

Contact Info

Product

Resources

About