The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens |
| |
| Authors: | Ildikó Nagy |
| |
| Institution: | Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, P.O. Box 7, Karolina út 29, H-1518, Hungary |
| |
| Abstract: | Cochlin is colocalized with type II collagen in the extracellular matrix of cochlea and has been suggested to interact with this collagen. Here we show that the second von Willebrand type A domain of cochlin has affinity for type II collagen, as well as type I and type IV collagens whereas the LCCL-domain of cochlin has no affinity for these proteins. The implications of these findings for the mechanism whereby cochlin mutations cause the dominant negative DFNA9-type hearing loss are discussed.Structured summary- MINT-6796048:
- type I collagen (uniprotkb:P02452) binds (MI:0407) to cochlin-vWA2 uniprotkb:O43405) by surface plasmon resonance (MI:0107)
- MINT-6796166:
- type III collagen (uniprotkb:P02462) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)
- MINT-6796062:
- type II collagen (uniprotkb:P02458) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)
|
| |
| Keywords: | Cochlin Collagen Deafness DFNA9 vWA domain |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
