1agg
From Proteopedia
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| - | [[Image:1agg.gif|left|200px]] | + | [[Image:1agg.gif|left|200px]] |
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| - | '''THE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTA''' | + | {{Structure |
| + | |PDB= 1agg |SIZE=350|CAPTION= <scene name='initialview01'>1agg</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTA''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AGG is a [ | + | 1AGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agelenopsis_aperta Agelenopsis aperta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGG OCA]. |
==Reference== | ==Reference== | ||
| - | The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta., Reily MD, Thanabal V, Adams ME, J Biomol NMR. 1995 Feb;5(2):122-32. PMID:[http:// | + | The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta., Reily MD, Thanabal V, Adams ME, J Biomol NMR. 1995 Feb;5(2):122-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7703698 7703698] |
[[Category: Agelenopsis aperta]] | [[Category: Agelenopsis aperta]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: p-type calcium channel antagonist]] | [[Category: p-type calcium channel antagonist]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:57:10 2008'' |
Revision as of 07:57, 20 March 2008
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THE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTA
Overview
The 48 amino acid peptides omega-Aga-IVA and omega-Aga-IVB are the first agents known to specifically block P-type calcium channels in mammalian brain, thus complementing the existing suite of pharmacological tools used for characterizing calcium channels. These peptides provide a new set of probes for studies aimed at elucidating the structural basis underlying the subtype specificity of calcium channel antagonists. We used 288 NMR-derived constraints in a protocol combining distance geometry and molecular dynamics employing the program DGII, followed by energy minimization with Discover to derive the three-dimensional structure of omega-Aga-IVB. The toxin consists of a well-defined core region, comprising seven solvent-shielded residues and a well-defined triple-stranded beta-sheet. Four loop regions have average backbone rms deviations between 0.38 and 1.31 A, two of which are well-defined type-II beta-turns. Other structural features include disordered C- and N-termini and several conserved basic amino acids that are clustered on one face of the molecule. The reported structure suggests a possible surface for interaction with the channel. This surface contains amino acids that are identical to those of another known P-type calcium channel antagonist, omega-Aga-IVA, and is rich in basic residues that may have a role in binding to the anionic sites in the extracellular regions of the calcium channel.
About this Structure
1AGG is a Single protein structure of sequence from Agelenopsis aperta. Full crystallographic information is available from OCA.
Reference
The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta., Reily MD, Thanabal V, Adams ME, J Biomol NMR. 1995 Feb;5(2):122-32. PMID:7703698
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