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Predicted full-length structure of human ZSCAN4 (433 residues), a zinc finger transcription factor with a SCAN dimerization domain and tandem C2H2 zinc finger array. ZSCAN4 is transiently expressed in two-cell-stage embryos and in a small subpopulation of mouse embryonic stem cells, where it has been implicated in telomere maintenance and genome stability during the totipotent state.
Predicted full-length structure of human LEUTX (198 residues), a paired-like homeodomain transcription factor expressed transiently during the first cleavage divisions of the human embryo. LEUTX is part of the embryonic genome activation network and its expression is rapidly silenced after the eight-cell stage.
Crystal structure of the human DUX4 transcription factor's tandem homeodomains in complex with a DNA duplex containing the consensus binding motif. Homeodomain 1 recognizes the TAA element via the canonical helix-in-major-groove contact, while homeodomain 2 reads the TGA element. DUX4 is the master regulator of zygotic genome activation in human embryos and is causally implicated in facioscapulohumeral muscular dystrophy (FSHD).
Classic 129-residue enzyme that cleaves bacterial cell walls. A long-standing benchmark for force-field validation and protein dynamics.
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
Closed-trimer prefusion conformation of the spike glycoprotein. The starting state for receptor-binding-domain opening dynamics.
Cas9 bound to a single-guide RNA and target DNA. The complete editing complex in a cleavage-ready geometry.
β2 adrenergic receptor captured coupled to its heterotrimeric Gs partner. A landmark GPCR signaling complex.
Twelve base pairs of canonical B-form DNA — the dodecamer that defined our picture of double-helix geometry.
The first protein structure ever solved by X-ray crystallography (Kendrew, 1958). Still a benchmark for oxygen-storage dynamics.
Human deoxyhemoglobin in the tense T state. Pairs naturally with 1HHO to study the allosteric switch behind cooperative oxygen binding.
Bovine rhodopsin in its dark resting state. A cornerstone for visual-pigment activation dynamics.
One of the few full-length immunoglobulin structures available — hinges, Fab arms, and Fc all resolved.
Src tyrosine kinase in its closed, autoinhibited conformation — the regulatory baseline that activation has to overcome.
PKA catalytic subunit bound to ATP and substrate peptide — the textbook reference structure for protein kinases.
A tetrameric water channel embedded in a plant plasma membrane. Each monomer gates water flow through a narrow selectivity filter.
147 base pairs of DNA wrapped around a histone octamer (two copies of H2A, H2B, H3, H4). The fundamental unit of chromatin.
Small, exceptionally stable Kunitz-domain inhibitor of serine proteases — one of the most thoroughly studied proteins in biophysics.
Seventy-six residues of fold-and-signaling perfection. The reference β-grasp fold and a staple of folding studies.