Publication Details |
Category | Text Publication |
Reference Category | Journals |
DOI | 10.1021/bi101187f |
Title (Primary) | A novel disulfide pattern in laminin-type epidermal growth factor-like (LE) modules of laminin β1 and γ1 chains |
Author | Kalkhof, S.; Witte, K.; Ihling, C.H.; Müller, M.Q.; Keller, M.V.; Haehn, S.; Smyth, N.; Paulsson, M.; Sinz, A. |
Source Titel | Biochemistry |
Year | 2010 |
Department | PROTEOM |
Volume | 49 |
Issue | 38 |
Page From | 8359 |
Page To | 8366 |
Language | englisch |
Supplements | https://pubs.acs.org/doi/suppl/10.1021/bi101187f/suppl_file/bi101187f_si_001.pdf |
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. |
Persistent UFZ Identifier | https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=10135 |
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 |