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Updated: Aug 17, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

SH3ドメインにおけるペプチド結合指向と配列特異性の構造的決定因子

W A Lim1, F M Richards, R O Fox

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114.

Nature
|November 24, 1994
PubMed
まとめ

SEM-5タンパク質のSrc-homology-3 (SH3) ドメインは,Sosペプチドを,以前に観察されたモードとは対照的な新しい方向で結合する. この二次モード結合メカニズムは,SH3ドメインを含む経路におけるシグナル特異性にとって極めて重要です.

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Protein Folding01:22

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Overview
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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.
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Ligand Binding Sites

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Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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