Results 241 to 250 of about 20,613 (283)

Serpin crystal structure and serpin polymer structure

Archives of Biochemistry and Biophysics, 2006
Serpins are a family of structurally homologous proteins having metastable native structures. As a result, a serpin variant destabilized by mutation(s) has a tendency to undergo conformational changes leading to inactive forms, e.g., the latent form and polymer. Serpin polymers are involved in a number of conformational diseases.
Ewa, Marszal, Andrew, Shrake
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Crystallography of Serpins and Serpin Complexes

2011
The serpin superfamily of protease inhibitors undergoes a remarkable conformational change to inhibit target proteases. To date, over 80 different serpin crystal structures have been determined. These data reveal that the serpin monomer can adopt five different conformations (native, partially inserted native, δ-form, latent, and cleaved).
M A, Dunstone, James C, Whisstock
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Serpin–ligand interactions

Methods, 2004
One of the more common features of serpins is the ability to bind various ligands. Ligand binding can occur so that the inhibitory properties of the serpin are regulated, so that the serpin can be localized, or to produce or modulate some other biological function of the serpin.
Philip A, Patston, Frank C, Church, Steven T, Olson   +2 more
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Serpin–Glycosaminoglycan Interactions

2011
Serpins (serine protease inhibitors) have traditionally been grouped together based on structural homology. They share common structural features of primary sequence, but not all serpins require binding to cofactors in order to achieve maximal protease inhibition. In order to obtain physiologically relevant rates of inhibition of target proteases, some
Chantelle M, Rein, Umesh R, Desai, Frank C, Church   +2 more
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Serpins (Serine Protease Inhibitors)

Current Protocols in Protein Science, 2001
AbstractSerpins are a class of proteins involved in the regulation of serine and other types of proteases. In humans, the majority of serpins regulate the functions of proteases involved in the body's response to injury. This includes roles in coagulation, fibrinolysis, inflammation, wound healing, and tissue repair.
Susannah J, Bauman, Herbert C, Whinna, Frank C, Church   +2 more
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Serpin tertiary structure transformation

Journal of Molecular Biology, 1991
Previous crystallographic analyses have demonstrated that proteolytic cleavage of the serpins can result in a dramatic transformation of their tertiary structure. Some 16 residues on the amino terminal side of the cleavage site are inserted into a large beta-sheet to become a central strand, separating the two cleaved residues by about 70 A.
P, Stein, C, Chothia
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Predicting Serpin/Protease Interactions

2011
Proteases are tightly regulated by specific inhibitors, such as serpins, which are able to undergo considerable and irreversible conformational changes in order to trap their targets. There has been a considerable effort to investigate serpin structure and functions in the past few decades; however, the specific interactions between proteases and ...
Jiangning, Song, Antony Y, Matthews, Cyril F, Reboul, Dion, Kaiserman, Robert N, Pike, Phillip I, Bird, James C, Whisstock   +6 more
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Serine protease inhibitors (serpins)

Trends in Cardiovascular Medicine, 1991
Inhibition of serine proteases by serpins (serpin: serine protease inhibitor) is a key mechanism for the control of proteolysis in thrombosis, shock, and inflammation. The various members of the serpin gene superfamily (α(1)-antitrypsin, ovalbumin, C1-inhibitor, antithrombin III, α(2)-antiplasmin, type-1 plasminogen-activator inhibitor, and so forth ...
M, Schapira, P A, Patston
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Solving Serpin Crystal Structures

2011
Essentially the same steps are required to solve the crystal structure of a serpin as for any other protein: produce and purify protein, grow crystals, collect diffraction data, find estimates of the phase angles, and then refine and validate the structure.
Randy J, Read, Aiwu, Zhou, Penelope E, Stein   +2 more
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Serpin Polymerization In Vitro

2011
Serpin polymerization is an event which generally occurs within living tissue as a consequence of a folding defect caused by point mutations. Major advances in cell biology and imaging have allowed detailed studies into subcellular localization, processing, and clearance of serpin polymers, but to understand the molecular basis of the misfolded state ...
James A, Huntington, Masayuki, Yamasaki
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