Topic
Globin fold
About: Globin fold is a research topic. Over the lifetime, 195 publications have been published within this topic receiving 14503 citations.
Papers published on a yearly basis
Papers
TL;DR: The crystal structure of the human retinoid-X receptor RXR-α ligand-binding domain reveals a previously undiscovered fold of an antiparallel α-helical sandwich, packed as dimeric units.
Abstract: The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.
1,213 citations
TL;DR: The identification of a third globin type in man and mouse that is predominantly expressed in the brain, and therefore called neuroglobin, represents a distinct protein family that diverged early in metazoan evolution, probably before the Protostomia/Deuterostomía split.
Abstract: Haemoglobins and myoglobins constitute related protein families that function in oxygen transport and storage in humans and other vertebrates. Here we report the identification of a third globin type in man and mouse. This protein is predominantly expressed in the brain, and therefore we have called it neuroglobin. Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 approximately 2 torr). Analogous to myoglobin, neuroglobin may increase the availability of oxygen to brain tissue. The human neuroglobin gene (NGB), located on chromosome 14q24, has a unique exon-intron structure. Neuroglobin represents a distinct protein family that diverged early in metazoan evolution, probably before the Protostomia/Deuterostomia split.
1,085 citations
TL;DR: The α/β hydrolase fold is a typical example of a tertiary fold adopted by proteins that have no obvious sequence similarity, but nevertheless, in the course of evolution, diverged from a common ancestor.
830 citations
TL;DR: The heme irons between hemoglobin and myoglobin and physical and chemical Criteria for Quaternary Structure and effects of quaternary structure on thermal spin equilibria are described.
Abstract: PERSPECTIVES AND SUMMARY 328 INTRODUCTION 330 STEREOCHEMISTRY OF IRON PORPHYRINS AND RELATED COMPOUNDS 332 Coordination of the Iron Atom 332 Interaction between Structure and Spin State in Iron Chelates 338 The Iron-Oxygen Bond 340 STEREOCHEMISTRY OF HEMOGLOBINS ".. 343 Monomeric and Dimeric Hemoglobins 343 Common tertiary structure ".. 343 Surroundings and structure of the heme in myoglobin.. ...... ........ ....... 344 Surroundings and structure of the heme in erythrocruorin 346 Tetrameric Hemoglobins 348 Changes in quaternary structure "... 349 Changes in tertiary structure 349 Significance of structural changes for ligand binding 353 Structural differences at the heme irons between hemoglobin and myoglobin 356 INTERACTIONS BETWEEN THE HEME AND THE GLOBIN 356 Physical and Chemical Criteria for Quaternary Structure 357 Methods of Changing Liganded Derivatives to the T Structure 359 Effects 0/ Changes in Quaternary Structure on the Heme 360 Deoxyhemoglobin 360 Liganded fe7roU!1 henwglobins ". 361 Ligandedferric henwglobins ,. 363 Effect of quaternary structure on thermal spin equilibria ........ ......... ........ ....... 366
680 citations
TL;DR: The S-adenosylmethionine-dependent methyltransferase enzymes share little sequence identity, but incorporate a highly conserved structural fold, and residues that bind the common cofactor are poorly conserved.
581 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 3 |
| 2018 | 2 |
| 2017 | 4 |
| 2016 | 4 |
| 2015 | 4 |
| 2014 | 5 |