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Crystal structure of a bacterial family‐III cellulose‐binding domain: a general mechanism for attachment to cellulose.
Although the proposed binding of the CBD to cellulose is essentially a surface interaction, specific types and combinations of amino acids appear to interact selectively with glucose moieties positioned on three adjacent chains of the cellulose surface.
Crystal Structure of the Hemochromatosis Protein HFE and Characterization of Its Interaction with Transferrin Receptor
It is demonstrated that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles, consistent with the demonstration that HFE, transferrin, and TFR form a ternary complex.
Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1.
- S. Smerdon, J. Jäger, +5 authors T. Steitz
- Biology, MedicineProceedings of the National Academy of Sciences…
- 26 April 1994
The co-crystal-structure of HIV-1 RT and Nevirapine has been solved previously at 3.5-A resolution and now is partially refined against data extending to 2.9-A spacing, implying that there may be limitations on the number of resistance mutations that yield viable virus.
Efficiency of signalling through cytokine receptors depends critically on receptor orientation
The crystal structure of erythropoietin complexed to the extracellular ligand-binding domains of the erymorphic receptor, determined at 1.9 Å from two crystal forms, shows that erythrooiet in imposes a unique 120° angular relationship and orientation that is responsible for optimal signalling through intracellular kinase pathways.
Three-dimensional structures of acidic and basic fibroblast growth factors.
Three-dimensional structures of two members of the fibroblast growth factor (FGF) family of proteins, bovine acidic FGF and human basic FGF, have been crystallographically determined and the locations of sequences implicated in receptor and heparin binding by FGF are presented.
Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions.
- T. Yeates, H. Komiya, A. Chirino, D. Rees, J. P. Allen, G. Feher
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 1 November 1988
The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R-26 and the wild-type strain 2.4.1…
Characterizing biological products and assessing comparability following manufacturing changes
Changes in production methods of a biological product may necessitate an assessment of comparability to ensure that these manufacturing changes have not affected the safety, identity, purity, or…
Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules.
Zn-alpha2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids. ZAG stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with…
Inactivation of TNF Signaling by Rationally Designed Dominant-Negative TNF Variants
Structural-based design is used to engineer variant TNF proteins that rapidly form heterotrimers with native TNF to give complexes that neither bind to nor stimulate signaling through TNF receptors, and TNF is inactivated by sequestration.
Rational design and engineering of therapeutic proteins.
- S. A. Marshall, G. Lazar, A. Chirino, J. Desjarlais
- Biology, MedicineDrug discovery today
- 1 March 2003
It is anticipated that rational protein engineering will shape the field of protein therapeutics dramatically by improving existing products and enabling the development of novel therapeutic agents.