التفاصيل البيبلوغرافية
| العنوان: |
Structure and properties of the Ca2+-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions. |
| المؤلفون: |
Christine Gaboriaud, Lynn Gregory‑Pauron, Florence Teillet, Nicole M. Thielens, Isabelle Bally, Gérard J. Arlaud |
| المصدر: |
Biochemical Journal; Oct2011, Vol. 439 Issue 2, p185-193, 9p |
| مصطلحات موضوعية: |
CALCIUM-binding proteins, PROTEIN structure, PROTEIN-protein interactions, EXTRACELLULAR matrix proteins, LOW density lipoproteins, MUTAGENESIS |
| مستخلص: |
CUB domains are 110-residue protein motifs exhibiting a β-sandwich fold and mediating protein–protein interactions in various extracellular proteins. Recent X-ray structural and mutagenesis studies have led to the identification of a particular CUB domain subset, cbCUB (Ca2+-binding CUB domain). Unlike other CUB domains, these harbour a homologous Ca2+-binding site that underlies a conserved binding site mediating ionic interaction between two of the three conserved acidic Ca2+ ligands and a basic (lysine or arginine) residue of a protein ligand, similar to the interactions mediated by the low-density lipoprotein receptor family. cbCUB-mediated protein–ligand interactions usually involve multipoint attachment through several cbCUBs, resulting in high-affinity binding through avidity, despite the low affinity of individual interactions. The aim of the present review is to summarize our current knowledge about the structure and functions of cbCUBs, which represent the majority of the known CUB repertoire and are involved in a variety of major biological functions, including immunity and development, as well as in various cancer types. Examples discussed in the present review include a wide range of soluble and membrane-associated human proteins, as well as some archaeal and invertebrate proteins. The fact that these otherwise unrelated proteins share a common Ca2+-dependent ligand-binding ability suggests a mechanism inheri-ted from very primitive ancestors. The information provided in the present review should stimulate further investigations on the crucial interactions mediated by cbCUB-containing proteins. [ABSTRACT FROM AUTHOR] |
|
Copyright of Biochemical Journal is the property of Portland Press Ltd. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
