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New page: '''Theoretical Model''' The entry 1T53 is a Theoretical Model titled 'ATP regulated module (ARM) domain of atrial natriuretic factor receptor guanylate cyclase'. [[Category:Theoretical M...
 
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'''Theoretical Model'''
{{Theoretical_model}}


The entry 1T53 is a Theoretical Model titled 'ATP regulated module (ARM) domain of atrial natriuretic factor receptor guanylate cyclase'.
==ATP REGULATED MODULE (ARM) DOMAIN OF ATRIAL NATRIURETIC FACTOR RECEPTOR GUANYLATE CYCLASE==
<StructureSection load='1t53' size='340' side='right'caption='[[1t53]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T53 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t53 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1t53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t53 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP is an obligatory agent for the atrial natriuretic factor (ANF) and the type C natriuretic peptide (CNP) signaling of their respective receptor guanylate cyclases, ANF-RGC and CNP-RGC. Through a common mechanism, it binds to a defined ARM domain of the cyclase, activates the cyclase and transduces the signal into generation of the second messenger cyclic GMP. In this presentation, the authors review the ATP-regulated transduction mechanism and refine the previously simulated three-dimensional ARM model (Duda T, Yadav P, Jankowska A, Venkataraman V, Sharma RK. Three dimensional atomic model and experimental validation for the ATP-regulated module (ARM) of the atrial natriuretic factor receptor guanylate cyclase. Mol Cell Biochem 2000;214:7-14; reviewed in: Sharma RK, Yadav P, Duda T. Allosteric regulatory step and configuration of the ATP-binding pocket in atrial natriuretic factor receptor guanylate cyclase transduction mechanism. Can J Physiol Pharmacol 2001;79: 682-91; Sharma RK. Evolution of the membrane guanylate cyclase transduction system. Mol Cell Biochem 2002;230:3-30). The model depicts the ATP-binding dependent configurational changes in the ARM and supports the concept that in the first step, ATP partially activates the cyclase and primes it for the subsequent transduction steps, resulting in full activation of the cyclase.


[[Category:Theoretical Model]]
ATP-regulated module (ARM) of the atrial natriuretic factor receptor guanylate cyclase.,Duda T, Venkataraman V, Ravichandran S, Sharma RK Peptides. 2005 Jun;26(6):969-84. Epub 2005 Apr 13. PMID:15911066<ref>PMID:15911066</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 13:28:41 2008''
</div>
<div class="pdbe-citations 1t53" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Theoretical Model]]
[[Category: Large Structures]]
[[Category: Duda, T]]
[[Category: Ravichandran, S]]
[[Category: Sharma, R K]]
[[Category: Venkataraman, V]]
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