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Crystal structure of the human prion protein reveals a mechanism for oligomerization
- K. Knaus, M. Morillas, W. Swietnicki, M. Malone, W. Surewicz, V. Yee
- Chemistry, BiologyNature Structural Biology
- 27 February 2002
The crystal structure of the human prion protein in dimer form at 2 Å resolution suggests that oligomerization through 3D domain-swapping may constitute an important step on the pathway of the PrPC → PrPSc conversion.
Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.
- V. Yee, L. Pedersen, I. Le Trong, P. Bishop, R. Stenkamp, D. Teller
- BiologyProceedings of the National Academy of Sciences…
- 19 July 1994
The three-dimensional structure of human recombinant factor XIII, a transglutaminase zymogen, has been solved at 2.8-A resolution by x-ray crystallography and a catalytic triad reminiscent of that observed in cysteine proteases has been identified in the core domain.
Blood coagulation factor XIII: structure and function.
Transglutaminase factor XIII uses proteinase‐like catalytic triad to crosslink macromolecules
- L. Pedersen, V. Yee, P. Bishop, I. L. Trong, D. Teller, R. Stenkamp
- Biology, ChemistryProtein science : a publication of the Protein…
- 1 July 1994
The X‐ray crystal structure of human transglutaminase factor XIII has revealed a cysteine proteinase‐like active site involved in a crosslinking reaction and not proteolysis. This is among the first…
Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase.
Identification of the Calcium Binding Site and a Novel Ytterbium Site in Blood Coagulation Factor XIII by X-ray Crystallography*
The x-ray crystal structure of recombinant factor XIII A2 in the presence of calcium, strontium, and ytterbium is determined, and the overall structure of ion-bound factor XIII is very similar to the previously determined crystal structures of factor XIII zymogen, likely due to the constraints of this monoclinic crystal form.
The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP.
- S. Iismaa, L. Chung, M. Wu, D. Teller, V. Yee, R. Graham
- Biology, ChemistryBiochemistry
- 30 September 1997
It is demonstrated that the GTP and ATP hydrolysis sites are localized within the core domain of TGase II and that neither the N-terminal beta-sandwich domain nor the C-terminally located beta-barrels are required for either GTP or ATP Hydrolysis.
Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution.
It is found that the cereal trypsin/alpha-amylase inhibitor family is evolutionarily related to the family of nonspecific lipid-transfer proteins of plants and apparently, the four-helix conformation has been a successful vehicle in plant evolution for providing protection from predators, food for the embryo, and lipid transfer.
Structure of the dimerized hormone-binding domain of a guanylyl- cyclase-coupled receptor
The crystal structure of the glycosylated dimerized hormone-binding domain of the ANP receptor is presented, a conserved chloride-binding site is located in the membrane distal domain, and it is found that hormone binding is chloride dependent.
Consequences of Seven Novel Mutations on the Expression and Structure of Keratinocyte Transglutaminase*
These results identify important amino acids in the central core domain of transglutaminases and show that the C-terminal end influences the structural and functional integrity of TGK.