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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...

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Structure and function of KH domains.

Roberto Valverde1, Laura Edwards, Lynne Regan

  • 1Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.

The FEBS Journal
|April 22, 2008
PubMed
Summary
This summary is machine-generated.

The K homology (KH) domain recognizes nucleic acids, binding RNA or ssDNA. Mutations in KH domains are linked to diseases like fragile X syndrome, highlighting their crucial cellular roles.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • The K homology (KH) domain is a nucleic acid-binding motif found in proteins regulating transcription and translation.
  • Dysfunction of KH domains is implicated in diseases such as fragile X mental retardation syndrome and paraneoplastic disease.

Purpose of the Study:

  • To review current understanding of KH domain molecular recognition of nucleic acids.
  • To discuss factors influencing nucleic acid binding affinity and specificity.
  • To explore the structural and functional significance of conserved residues and mutations within KH domains.

Main Methods:

  • Literature review of studies on KH domain structure and function.
  • Analysis of binding interactions, including forces and typical binding site characteristics.
  • Discussion of strategies for enhancing binding affinity and specificity, such as 'augmented' domains or multiple copies.
  • Examination of crystallization data and solution behavior of KH domains.
  • Review of mutation studies, particularly concerning conserved hydrophobic residues.

Main Results:

  • KH domains typically bind RNA or single-stranded DNA (ssDNA) in a cleft accommodating approximately four unpaired bases.
  • Binding affinity is influenced by Van der Waals forces, hydrophobic interactions, and electrostatic interactions.
  • Multiple KH domains or 'augmented' domains enhance binding affinity and specificity.
  • While isolated KH domains crystallize as monomers, dimers, or tetramers, higher-order oligomers in solution are not supported by current data.
  • A specific mutation (Ile to Asn) in the fragile X mental retardation protein KH2 domain leads to a severe disease phenotype, underscoring the importance of conserved residues.

Conclusions:

  • KH domains are versatile nucleic acid-binding modules critical for various cellular processes.
  • Understanding the structure-function relationship of KH domains, including the impact of specific mutations, is vital for deciphering their roles in health and disease.
  • Further research using point mutations can elucidate the precise mechanisms of KH domain-mediated nucleic acid recognition and regulation.