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1apq
From Proteopedia
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| - | [[Image:1apq.gif|left|200px]]<br /><applet load="1apq" size=" | + | [[Image:1apq.gif|left|200px]]<br /><applet load="1apq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1apq" /> | caption="1apq" /> | ||
'''STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES'''<br /> | '''STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1APQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Known structural/functional Site: <scene name='pdbsite=CAB:prob. Ca Binding Site'>CAB</scene>. Full crystallographic information is available from [http:// | + | 1APQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Known structural/functional Site: <scene name='pdbsite=CAB:prob.+Ca+Binding+Site'>CAB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:31:14 2008'' |
Revision as of 07:31, 3 February 2008
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STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES
Contents |
Overview
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 calculations. The resulting family, of 19 structures is characterized by a well-ordered C-terminal part, (residues Cys 144-Ala174) with a backbone rmsd of 0.7 A and a disordered, N-terminal, including the large loop between the first two cysteines, (Cys129 and Cys144). This loop is known to be surface exposed and may be, expected to participate in domain-domain or protein-protein interactions., In its C-terminal part, C1r-EGF possesses the characteristic EGF fold with, a major and a minor beta-sheet. The latter comprises a beta-bulge, and, comparison with other EGF-like modules reveals the existence of two, distinct structural and sequential motifs in the bulged part. Additional, experiments in the presence of 80 mM Ca2+ did not show significant, structural variation of C1r-EGF, in keeping with previous observations on, blood-clotting factors IX and X.
Disease
Known disease associated with this structure: C1r/C1s deficiency, combined OMIM:[216950]
About 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 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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