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2m3s

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'''Unreleased structure'''
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{{STRUCTURE_2m3s| PDB=2m3s | SCENE= }}
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===Calmodulin, i85l, f92e, h107i, l107i, a128t, m144r mutant===
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{{ABSTRACT_PUBMED_23630096}}
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The entry 2m3s is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
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Authors: Moroz, Y.S., Wu, Y., Cheng, H., Roder, H., Korendovych, I.V.
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==About this Structure==
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[[2m3s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3S OCA].
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Description: Calmodulin, i85l, f92e, h107i, l107i, a128t, m144r mutant
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==Reference==
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<ref group="xtra">PMID:023630096</ref><references group="xtra"/><references/>
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[[Category: Gallus gallus]]
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[[Category: Cheng, H.]]
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[[Category: Korendovych, I V.]]
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[[Category: Moroz, Y S.]]
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[[Category: Roder, H.]]
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[[Category: Wu, Y.]]
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[[Category: Calmodulin]]
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[[Category: Metal binding protein]]

Revision as of 12:58, 24 July 2013

Template:STRUCTURE 2m3s

Contents

Calmodulin, i85l, f92e, h107i, l107i, a128t, m144r mutant

Template:ABSTRACT PUBMED 23630096

Function

[CALM_CHICK] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.

About this Structure

2m3s is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA.

Reference

  • Moroz OV, Moroz YS, Wu Y, Olsen AB, Cheng H, Mack KL, McLaughlin JM, Raymond EA, Zhezherya K, Roder H, Korendovych IV. A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction. Angew Chem Int Ed Engl. 2013 Jun 10;52(24):6246-9. doi: 10.1002/anie.201302339., Epub 2013 Apr 29. PMID:23630096 doi:10.1002/anie.201302339

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OCA

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