期刊
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
卷 25, 期 4-5, 页码 351-358出版社
SPRINGER
DOI: 10.1007/s10974-004-0690-7
关键词
actin; calponin; CH-domains; dystrophin; utrophin
类别
资金
- NHLBI NIH HHS [HL62468, HL36153] Funding Source: Medline
- NIAMS NIH HHS [AR34711] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL036153, R55HL036153, R37HL036153, R01HL062468] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [R01AR034711] Funding Source: NIH RePORTER
Calponin homology domains link many different proteins to the surface of actin filaments. However. details of the structural interactions involved and the methods used to determine them are controversial. In the case of the actin-binding protein utrophin, for example, several models have been proposed for the binding of utrophin's calponin homology domains to actin. We review and evaluate these models and their supporting data.
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