Details zur Publikation
Kategorie Textpublikation
Referenztyp Zeitschriften
DOI 10.1021/bi101187f
Titel (primär) A novel disulfide pattern in laminin-type epidermal growth factor-like (LE) modules of laminin β1 and γ1 chains
Autor Kalkhof, S.; Witte, K.; Ihling, C.H.; Müller, M.Q.; Keller, M.V.; Haehn, S.; Smyth, N.; Paulsson, M.; Sinz, A.
Quelle Biochemistry
Erscheinungsjahr 2010
Department PROTEOM
Band/Volume 49
Heft 38
Seite von 8359
Seite bis 8366
Sprache englisch
Supplements Supplement 1
Keywords laminin; epidermal growth factor; disulfide bond; mass spectrometry
Abstract In-depth mass spectrometric analysis of disulfide bond patterns in recombinant mouse laminin s1 and ã1 chain N-terminal fragments comprising the laminin N-terminal (LN)domain and the first four laminin epidermal growth factor-like (LE) domains revealed a novel disulfide pattern for LE domains. This showed a (2-3, 4-5, 6-7, 8-1) connectivity with the last cysteine of one LE domain being connected to the first cysteine of the following LE domain. The same pattern was also found in E4, the N-terminal â1 chain fragment derived by elastase digestion of mouse EHS tumor laminin-111, showing that this pattern occurs in native laminin. The strictly linear pattern with an interdomain disulfide has not been described previously for EGF domains. The N-terminal portions of laminin short arms, consisting of the LN domain and LE domains 1-4 are essential for laminin-laminin self interactions, whereas the internal LE domains 7-9 in the laminin ã1 chain harbor the nidogen binding site and have a conventional disulfide pattern. This suggests that LE domains differing in function also differ in their disulfide patterns.
Kalkhof, S., Witte, K., Ihling, C.H., Müller, M.Q., Keller, M.V., Haehn, S., Smyth, N., Paulsson, M., Sinz, A. (2010):
A novel disulfide pattern in laminin-type epidermal growth factor-like (LE) modules of laminin β1 and γ1 chains
Biochemistry 49 (38), 8359 - 8366 10.1021/bi101187f