Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses 1 1Edited by R. Huber

Aw, Ashton; Mk, Boehm; Gallimore,; Pepys, MB; Perkins, SJ

doi:10.1006/jmbi.1997.1271

Cited by 111 publications

(115 citation statements)

References 45 publications

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“…Although trimeric PTXs exist in fish (Huong Giang et al, 2010), this is the first report on the crystal structure of a bony fish PTX. The trimeric structure differs from reported pentraxin structures, such as classical pentameric hCRP, hSAP, decameric hSAP and hCRP (Ashton et al, 1997;Hohenester et al, 1997) as well as doubly stacked heptameric and octameric limulus SAP-like pentraxin ( Fig. 1B and C).…”

Section: Dare-ptx Is a Trimermentioning

confidence: 61%

Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces

Chen

Yuan

et al. 2015

Journal of Structural Biology

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Section: Dare-ptx Is a Trimermentioning

confidence: 61%

Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces

Chen

Yuan

et al. 2015

Journal of Structural Biology

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“…A nominal resolution of the data is 1.2 nm, and details of the tertiary structure can obviously not be validated experimentally at this level of resolution, which is why we restricted ourselves to rigid body modeling. Solution scattering is rather sensitive to rigid body movements of structural domains and has successfully been used to model the quaternary structure of proteins (15)(16)(17). The use of rigid body modeling is justified by a high sequence homology between monomeric ␣B-crystallin and MjHSP16.5.…”

Section: Discussionmentioning

confidence: 99%

A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity

Feil¹,

Malfois²,

Hendle³

et al. 2001

Journal of Biological Chemistry

105

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␣B-crystallin, a member of the small heat-shock protein family and a major eye lens protein, is a high molecular mass assembly and can act as a molecular chaperone. We report a synchrotron radiation x-ray solution scattering study of a truncation mutant from the human ␣B-crystallin (␣B57-157), a dimeric protein that comprises the ␣-crystallin domain of the ␣B-crystallin and retains a significant chaperone-like activity. According to the sequence analysis (more than 23% identity), the monomeric fold of the ␣-crystallin domain should be close to that of the small heat-shock protein from Methanococcus jannaschii (MjHSP16.5). The theoretical scattering pattern computed from the crystallographic model of the dimeric MjHSP16.5 deviates significantly from the experimental scattering by the ␣-crystallin domain, pointing to different quaternary structures of the two proteins. A rigid body modeling against the solution scattering data yields a model of the ␣-crystallin domain revealing a new dimerization interface. The latter consists of a strand-turn-strand motif contributed by each of the monomers, which form a four-stranded, antiparallel, intersubunit composite ␤-sheet. This model agrees with the recent spin labeling results and suggests that the ␣B-crystallin is composed by flexible building units with an extended surface area. This flexibility may be important for biological activity and for the formation of ␣B-crystallin complexes of variable sizes and compositions.␣A-and ␣B-crystallin, which share 54% amino acid sequence identity, build the subunits of ␣-crystallin, a major eye lens protein, comprising up to 40% of the total lens proteins. The structural function of the ␣-crystallin is to assist in maintaining transparency in the lens (1). The chaperone-like function of ␣B-crystallin helps to avoid formation of large light-scattering aggregates and possibly helps to prevent cataract in the lens. Moreover, neurodegenerative diseases, ischemia, or multiple sclerosis lead to an overexpression of this protein, which makes it an object of special medical interest (2).The ␣-crystallin as well as other mammalian small heat-shock proteins (sHSPs)1 form large globular complexes with a diameter of about 10 -25 nm. Cryoelectron microscopy and image analysis revealed that ␣B-crystallin is a hollow spherical shell with variable quaternary structure (3), and a frequent exchange of subunits between the particles was observed. The chaperone activity of ␣B-crystallin is associated with partial perturbation of the substrate protein tertiary structure, leading to a multimeric molten globule-like state with increased hydrophobicity (4, 5). The exposed hydrophobic regions of ␣-crystallin interact with substrate proteins possessing an increased surface hydrophobicity but a low degree of unfolding (6).The molecular structure and subunit interactions in ␣-crystallin have long been under investigation. The stretches of residues promoting formation of lower or higher molecular weight ␣-crystallin oligomers have been identified. Upon additio...

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“…The direct conversion of the atomic coordinate model into small spheres is one approach. The sphere model (also known as a 'bead' model) has to include a hydration shell of spheres, so this is the same hydrated model as that used for X-ray scattering fits (Ashton et al 1997). The models are submitted to HYDRO software to calculate the s 0 20,w value (Garcia de la Torre et al 1994).…”

Section: Analytical Ultracentrifugation and Modellingmentioning

confidence: 99%

Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights

Perkins

Okemefuna

Nan

et al. 2009

J. R. Soc. Interface.

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X-ray and neutron-scattering techniques characterize proteins in solution and complement high-resolution structural studies. They are useful when either a large protein cannot be crystallized, in which case scattering yields a solution structure, or a crystal structure has been determined and requires validation in solution. These solution structures are determined by the application of constrained modelling methods based on known subunit structures. First, an appropriate starting model is generated. Next, its conformation is randomized to generate thousands of models for trial-and-error fits. Comparison with the experimental data identifies a small family of best-fit models. Finally, their significance for biological function is assessed. We illustrate this in application to structure determinations for secretory immunoglobulin A, the most prevalent antibody in the human body and a first line of defence in mucosal immunity. We also discuss the applications to the large multi-domain proteins of the complement system, most notably its major regulator factor H, which is important in age-related macular degeneration and renal diseases. We discuss the importance of complementary data from analytical ultracentrifugation, and structural studies of protein -protein complexes. We conclude that constrained scattering modelling makes useful contributions to our understanding of antibody and complement structure and function.

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Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses 1 1Edited by R. Huber

Cited by 111 publications

References 45 publications

Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces

Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces

A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity

Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights

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