scholarly journals Structure and Function of Cytochromes P450 2B: From Mechanism-Based Inactivators to X-Ray Crystal Structures and Back

2011 ◽  
Vol 39 (7) ◽  
pp. 1113-1121 ◽  
Author(s):  
James R. Halpert
Keyword(s):  
Crystal Structures ◽  
Cytochromes P450 ◽  
Structure And Function ◽  
X Ray ◽  
And Function

Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

1999 ◽  
Vol 82 (08) ◽  
pp. 271-276 ◽  
Author(s):  
Glen Spraggon ◽  
Stephen Everse ◽  
Russell Doolittle
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Crystal Structures ◽  
Structure And Function ◽  
X Ray ◽  
Long Period ◽  
And Function

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

scholarly journals Structure and function of cytochromes P450:a comparative analysis of three crystal structures

Structure ◽  
1995 ◽  
Vol 3 (1) ◽  
pp. 41-62 ◽  
Author(s):  
Charles A Hasemann ◽  
Ravi G Kurumbail ◽  
Sekhar S Boddupalli ◽  
Julian A Peterson ◽  
Johann Deisenhofer
Keyword(s):  
Comparative Analysis ◽  
Crystal Structures ◽  
Cytochromes P450 ◽  
Structure And Function ◽  
And Function

scholarly journals Structures of TOG1 and TOG2 From the Human Microtubule Dynamics Regulator CLASP1

2018 ◽  
Author(s):  
Jonathan B. Leano ◽  
Kevin C. Slep
Keyword(s):  
Crystal Structures ◽  
Family Members ◽  
Structural Diversity ◽  
Binding Activity ◽  
Structure And Function ◽  
Microtubule Dynamics ◽  
Structural Elements ◽  
X Ray ◽  
Tubulin Binding ◽  
And Function

AbstractTubulin-binding TOG domains are found arrayed in a number of proteins that regulate microtubule dynamics. While much is known about the structure and function of TOG domains in the XMAP215 microtubule polymerase family, less in known about the TOG domain array found in the CLASP family. The CLASP TOG array promotes microtubule pause, potentiates rescue, and limits catastrophe. How distinct the TOG domains of CLASP are from one another, from XMAP215 TOG domains, and whether they are positionally conserved across CLASP family members is poorly understood. We present the x-ray crystal structures of human CLASP1 TOG1 and TOG2. The structures of CLASP1 TOG1 and TOG2 are distinct from each other, from CLASP TOG3, and are positionally conserved across species. While studies have failed to detect CLASP TOG1 tubulin-binding activity, TOG1 is structurally similar to the free-tubulin binding TOG domains of XMAP215. In contrast, though CLASP TOG2 and TOG3 have tubulin binding activity, they are structurally distinct from the free-tubulin binding TOG domains of XMAP215. CLASP TOG2 has a convex architecture, predicted to engage a hyper-curved tubulin state. CLASP TOG3 has unique structural elements in the C-terminal half of its α-solenoid domain that modeling studies implicate in binding to laterally-associated tubulin subunits in the microtubule lattice in a mode similar to, yet distinct from XMAP215 TOG4. These findings highlight the structural diversity of TOG domains within the CLASP TOG array and provide a molecular foundation for understanding CLASP-dependent effects on microtubule dynamics.

scholarly journals Betp - X-Ray Structure and Function of An Osmosensor and Transporter

2010 ◽  
Vol 98 (3) ◽  
pp. 46a
Author(s):  
Reinhard Kraemer ◽  
Susanne Ressl ◽  
Vera Ott ◽  
Sascha Nicklisch ◽  
Heinz-Juergen Steinhoff ◽  
...  
Keyword(s):  
Structure And Function ◽  
X Ray ◽  
And Function

scholarly journals General discussion summary

2002 ◽  
Vol 357 (1426) ◽  
pp. 1419-1420 ◽  
Keyword(s):  
Water Splitting ◽  
Molecular Mechanisms ◽  
Structure And Function ◽  
X Ray ◽  
X Ray Crystallography ◽  
And Function ◽  
Splitting Process

This general discussion was chaired by A. W. Rutherford ( Service de Bioénergétique, Saclay, France ) and revolved around two major topics: (i) the implications of X–ray crystallography on the relationships between structure and function; (ii) the molecular mechanisms of the water–splitting process.

Feeding Structures and their Functions in Adult and Preadult Tigriopus Californicus (Copepoda: Harpacticoida)

1998 ◽  
Vol 78 (2) ◽  
pp. 451-466 ◽  
Author(s):  
A.G. Lewis ◽  
L. Chatters ◽  
M. Raudsepp
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Structure And Function ◽  
Energy Dispersive ◽  
Tigriopus Californicus ◽  
X Ray ◽  
Faecal Pellets ◽  
Spinous Processes ◽  
And Function ◽  
Scanning Electron

Tigriopus californicus uses several appendages and processes in the collection and manipulation of food. Their structure and function appear to enable the species to utilize the variety of food materials found in splashpools, including: detritus and organic floes; superficial material on particles; faecal pellets; protists; diatoms; and small crustaceans. From light and scanning electron microscopy and video, the labrum and labium appear to be adapted for biting soft and hard food materials and holding food for trituration by the mandibles. From energy dispersive X-ray spectra, the gnathobase of the mandible is suggested to be sclerotized but not calcified or silicified. It has an array of bilobate and multilobate teeth, clusters of spinous processes, and a heavy, spine-bearing process to move food into the oesophagus. There is also a flange which articulates in a groove in the labrum which appears to provide a guide for the gnathobase as it moves vertically.

scholarly journals Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function

2017 ◽  
Vol 34 (9) ◽  
pp. 1141-1172 ◽  
Author(s):  
Jeffrey D. Rudolf ◽  
Chin-Yuan Chang ◽  
Ming Ma ◽  
Ben Shen
Keyword(s):  
Natural Products ◽  
Natural Product ◽  
Cytochromes P450 ◽  
Structure And Function ◽  
Sequence Structure ◽  
Natural Product Biosynthesis ◽  
And Function

This review catalogues functionally characterized P450s fromStreptomycesand discusses their sequences, structures, and functions in natural products biosynthesis.

Sign in / Sign up

Export Citation Format

Share Document