2lyw

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[[Image:2lyw.jpg|left|200px]]
 
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{{STRUCTURE_2lyw| PDB=2lyw | SCENE= }}
{{STRUCTURE_2lyw| PDB=2lyw | SCENE= }}
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===Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor===
===Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor===
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{{ABSTRACT_PUBMED_23140271}}
{{ABSTRACT_PUBMED_23140271}}
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==Function==
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[[http://www.uniprot.org/uniprot/NTR1_HUMAN NTR1_HUMAN]] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. [[http://www.uniprot.org/uniprot/NEUT_HUMAN NEUT_HUMAN]] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.
==About this Structure==
==About this Structure==
[[2lyw]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LYW OCA].
[[2lyw]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LYW OCA].
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==Reference==
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<ref group="xtra">PMID:023140271</ref><references group="xtra"/><references/>
[[Category: Costa, G Da.]]
[[Category: Costa, G Da.]]
[[Category: Monti, J.]]
[[Category: Monti, J.]]

Revision as of 11:22, 24 July 2013

Template:STRUCTURE 2lyw

Contents

Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor

Template:ABSTRACT PUBMED 23140271

Function

[NTR1_HUMAN] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. [NEUT_HUMAN] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.

About this Structure

2lyw is a 2 chain structure. Full experimental information is available from OCA.

Reference

  • Da Costa G, Bondon A, Coutant J, Curmi P, Monti JP. Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor. J Biomol Struct Dyn. 2012 Nov 12. PMID:23140271 doi:10.1080/07391102.2012.736776

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