1agg: Difference between revisions

Revision as of 16:47, 30 June 2008

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File:1agg.png

Template:STRUCTURE 1agg

THE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTATHE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTA

Template:ABSTRACT PUBMED 7703698

About this StructureAbout this Structure

1AGG is a Single protein structure of sequence from Agelenopsis aperta. Full experimental information is available from OCA.

ReferenceReference

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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-'''THE SOLUTION STRUCTURE OF OMEGA-AGA-IVB, A P-TYPE CALCIUM CHANNEL ANTAGONIST FROM THE VENOM OF AGELENOPSIS APERTA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7703698}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7703698 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7703698}}
 ==About this Structure==
-AGG 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].
+AGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agelenopsis_aperta Agelenopsis aperta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGG OCA].
 ==Reference==
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 [[Category: Neurotoxin]]
 [[Category: P-type calcium channel antagonist]]
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