1n4k: Difference between revisions

Revision as of 13:51, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n4k.png

Template:STRUCTURE 1n4k

Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3

Template:ABSTRACT PUBMED 12442173

About this StructureAbout this Structure

1N4K is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand., Bosanac I, Alattia JR, Mal TK, Chan J, Talarico S, Tong FK, Tong KI, Yoshikawa F, Furuichi T, Iwai M, Michikawa T, Mikoshiba K, Ikura M, Nature. 2002 Dec 12;420(6916):696-700. Epub 2002 Nov 17. PMID:12442173

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OCA

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 {{STRUCTURE_1n4k|  PDB=1n4k  |  SCENE=  }}
-'''Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3'''
+===Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3===
-==Overview==
+<!--
-In a variety of cells, the Ca2+ signalling process is mediated by the endoplasmic-reticulum-membrane-associated Ca2+ release channel, inositol 1,4,5-trisphosphate (InsP3) receptor (InsP3R). Being ubiquitous and present in organisms ranging from humans to Caenorhabditis elegans, InsP3R has a vital role in the control of cellular and physiological processes as diverse as cell division, cell proliferation, apoptosis, fertilization, development, behaviour, memory and learning. Mouse type I InsP3R (InsP3R1), found in high abundance in cerebellar Purkinje cells, is a polypeptide with three major functionally distinct regions: the amino-terminal InsP3-binding region, the central modulatory region and the carboxy-terminal channel region. Here we present a 2.2-A crystal structure of the InsP3-binding core of mouse InsP3R1 in complex with InsP3. The asymmetric, boomerang-like structure consists of an N-terminal beta-trefoil domain and a C-terminal alpha-helical domain containing an 'armadillo repeat'-like fold. The cleft formed by the two domains exposes a cluster of arginine and lysine residues that coordinate the three phosphoryl groups of InsP3. Putative Ca2+-binding sites are identified in two separate locations within the InsP3-binding core.
+The line below this paragraph, {{ABSTRACT_PUBMED_12442173}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12442173 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12442173}}
 ==About this Structure==
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 [[Category: Ip3 receptor]]
 [[Category: Ip3-binding core]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:05:13 2008''
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