From Proteopedia
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| - | [[Image:1apq.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1apq| PDB=1apq | SCENE= }} | | {{STRUCTURE_1apq| PDB=1apq | SCENE= }} |
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| - | '''STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES'''
| + | ===STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9477945}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9477945 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9477945}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1APQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APQ OCA]. | + | 1APQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APQ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Egf]] | | [[Category: Egf]] |
| | [[Category: Serine protease]] | | [[Category: Serine protease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:33:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:22:10 2008'' |
Revision as of 14:22, 30 June 2008
Template:STRUCTURE 1apq
STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES
Template:ABSTRACT PUBMED 9477945
About this Structure
1APQ is a Single protein structure of sequence from Homo sapiens. Full experimental 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
Page seeded by OCA on Mon Jun 30 17:22:10 2008
