1apq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 24: | Line 24: | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14: | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:50:33 2007'' | ||
Revision as of 15:45, 30 October 2007
|
STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES
OverviewOverview
The calcium-dependent interaction between C1r and C1s, the two homologous, serine proteases of the first component of human complement C1, is, mediated by their N-terminal regions. The latter comprise an epidermal, growth factor (EGF)-like module exhibiting the consensus sequence, characteristic of Ca(2+)-binding EGF modules, surrounded by two CUB, modules. Due to its Ca2+ binding ability, the C1r EGF-like module, (C1r-EGF) is supposed to participate in the C1r-C1s interaction. An, additional interesting feature of C1r-EGF is the unusually large loop, connecting the first two conserved cysteine residues. The solution, structure of synthetic C1r-EGF (residues 123-175) has been determined, using nuclear magnetic resonance and combined simulated, annealing-restrained molecular dynamics ... [(full description)]
About this StructureAbout this Structure
1APQ is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Complement subcomponent C1r], with EC number [3.4.21.41]. Structure known Active Site: CAB. Full crystallographic information is available from [OCA].
ReferenceReference
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family., Bersch B, Hernandez JF, Marion D, Arlaud GJ, Biochemistry. 1998 Feb 3;37(5):1204-14. PMID:9477945
Page seeded by OCA on Tue Oct 30 14:50:33 2007