3c16: Difference between revisions

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{{Seed}}
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[[Image:3c16.jpg|left|200px]]
[[Image:3c16.png|left|200px]]


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===Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca===
===Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca===


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{{ABSTRACT_PUBMED_19243146}}


==About this Structure==
==About this Structure==
3C16 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C16 OCA].  
3C16 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C16 OCA].  
==Reference==
<ref group="xtra">PMID:19243146</ref><references group="xtra"/>
[[Category: Adenylate cyclase]]
[[Category: Adenylate cyclase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Transmembrane]]
[[Category: Transmembrane]]


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Revision as of 05:55, 13 May 2009

File:3c16.png

Template:STRUCTURE 3c16

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca

Template:ABSTRACT PUBMED 19243146

About this Structure

3C16 is a 3 chains structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

  1. Mou TC, Masada N, Cooper DM, Sprang SR. Structural basis for inhibition of mammalian adenylyl cyclase by calcium. Biochemistry. 2009 Apr 21;48(15):3387-97. PMID:19243146 doi:https://dx.doi.org/10.1021/bi802122k

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