The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens

Autor:	Nagy, Ildikó, Trexler, Mária, Patthy, László
Předmět:	VON Willebrand disease COLLAGEN EXTRACELLULAR matrix proteins COCHLEA GENETIC mutation DEAFNESS
Zdroj:	FEBS Letters; Dec2008, Vol. 582 Issue 29, p4003-4007, 5p
Abstrakt:	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) [Copyright &y& Elsevier]
Databáze:	Complementary Index
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