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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
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Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Central Nervous System Tumors in Xeroderma Pigmentosum: Five Cases and Review of the Literature.

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A Splicing Variant in XPA Results in Delayed Onset of Clinical Features of Xeroderma Pigmentosum.

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TFIIH-p52ΔC defines a ninth xeroderma pigmentosum complementation-group XP-J and restores TFIIH stability to p8-defective trichothiodystrophy.

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Clinical and molecular overlap between nucleotide excision repair (NER) disorders and <i>DYRK1A</i> haploinsufficiency syndrome.

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Updated: Jul 2, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
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Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

XPD structure reveals its secrets.

Alan R Lehmann1

  • 1Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton, UK. a.r.lehmann@sussex.ac.uk

DNA Repair
|August 12, 2008
PubMed
Summary
This summary is machine-generated.

Crystal structures of the XPD protein reveal novel domains and a 4FeS cluster. These findings advance our understanding of DNA repair deficiencies and associated human disorders, linking XPD gene variations to disease.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • The Xeroderma pigmentosum group D (XPD) protein is crucial for DNA repair pathways, particularly nucleotide excision repair (NER).
  • Deficiencies in NER, often linked to XPD dysfunction, are associated with various human genetic disorders and increased cancer susceptibility.
  • Understanding XPD's structure-function relationship is key to deciphering these genotype-phenotype correlations.

Purpose of the Study:

  • To elucidate the structural basis of XPD protein function.
  • To provide insights into the mechanisms underlying NER pathway fidelity.
  • To correlate structural findings with known XPD-related human diseases.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structures of archaeal XPD.
  • Comparative structural analysis was performed to identify conserved and novel domains.
  • Bioinformatic tools were utilized to analyze protein domains and their potential functions.

Main Results:

  • The crystal structures revealed the presence of canonical helicase domains alongside a novel "Arch" domain.
  • A unique 4FeS cluster was identified within the XPD structure, suggesting roles beyond simple DNA unwinding.
  • Structural data provides a framework for interpreting mutations and their impact on XPD function.

Conclusions:

  • The newly identified structural features of XPD offer novel insights into its catalytic mechanisms and interactions.
  • These structural findings are instrumental in understanding the molecular basis of XPD-related disorders.
  • The study enhances our comprehension of genotype-phenotype relationships in the context of the XPD gene and NER pathway.