2rcz
From Proteopedia
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- | [[Image:2rcz.jpg|left|200px]] | + | [[Image:2rcz.jpg|left|200px]] |
- | + | ||
- | '''Structure of the second PDZ domain of ZO-1''' | + | {{Structure |
+ | |PDB= 2rcz |SIZE=350|CAPTION= <scene name='initialview01'>2rcz</scene>, resolution 1.700Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= TJP1, ZO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Structure of the second PDZ domain of ZO-1''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2RCZ is a [ | + | 2RCZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCZ OCA]. |
==Reference== | ==Reference== | ||
- | Domain swapping within PDZ2 is responsible for dimerization of ZO proteins., Fanning AS, Lye MF, Anderson JM, Lavie A, J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:[http:// | + | Domain swapping within PDZ2 is responsible for dimerization of ZO proteins., Fanning AS, Lye MF, Anderson JM, Lavie A, J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17928286 17928286] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tight junction]] | [[Category: tight junction]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:34:56 2008'' |
Revision as of 16:34, 20 March 2008
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, resolution 1.700Å | |||||||
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Gene: | TJP1, ZO1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of the second PDZ domain of ZO-1
Overview
ZO-1 is a multidomain protein involved in cell-cell junctions and contains three PDZ domains, which are necessary for its function in vivo. PDZ domains play a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins. We determined the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins. The dimer is stabilized by extensive symmetrical domain swapping of beta-strands, which is unlike any other known mechanism of PDZ dimerization. The canonical peptide-binding groove remains intact in both subunits of the PDZ2 dimer and is created by elements contributed from both monomers. This unique structure reveals an additional example of how PDZ domains dimerize and has multiple implications for both peptide binding and oligomerization in vivo.
About this Structure
2RCZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Domain swapping within PDZ2 is responsible for dimerization of ZO proteins., Fanning AS, Lye MF, Anderson JM, Lavie A, J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:17928286
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