Structural consequences of cysteine substitutions C1977Y and C1977R in calcium-binding epidermal growth factor-like domain 30 of human fibrillin-1.
The largest group of disease-causing mutations affecting calcium-binding epidermal growth factor-like (cbEGF) domain function in a wide variety of extracellular and transmembrane proteins is that which results in cysteine substitutions. Although known to introduce proteolytic susceptibility, the det...
Main Authors: | Suk, J, Jensen, S, McGettrick, A, Willis, A, Whiteman, P, Redfield, C, Handford, P |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2004
|
Similar Items
-
Fibrillin-1 misfolding and disease.
by: Whiteman, P, et al.
Published: (2006) -
¹H, ¹³C and ¹⁵N assignments of the four N-terminal domains of human fibrillin-1.
by: Yadin, D, et al.
Published: (2014) -
Ca2+-dependent interface formation in fibrillin-1.
by: Jensen, SA, et al.
Published: (2005) -
Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.
by: Whiteman, P, et al.
Published: (2007) -
Case report: Biochemical and clinical phenotypes caused by cysteine substitutions in the epidermal growth factor-like domains of fibrillin-1
by: Xin Liu, et al.
Published: (2022-08-01)