Journal article icon

Journal article

NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1.

Abstract:

EMILIN1 is a glycoprotein of elastic tissues that has been recently linked to the pathogenesis of hypertension. The protein is formed by different independently folded structural domains whose role has been partially elucidated. In this paper the solution structure, inferred from NMR-based homology modelling of the C-terminal trimeric globular C1q domain (gC1q) of EMILIN1, is reported. The high molecular weight and the homotrimeric structure of the protein required the combined use of highly ...

Expand abstract

Actions


Access Document


Publisher copy:
10.1007/s10858-008-9290-y

Authors


Verdone, G More by this author
Corazza, A More by this author
Colebrooke, SA More by this author
Expand authors...
Journal:
Journal of biomolecular NMR
Volume:
43
Issue:
2
Pages:
79-96
Publication date:
2009-02-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:be5f8a2a-c982-4f9d-9634-8bf8b01616f4
Source identifiers:
246517
Local pid:
pubs:246517

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP