2jte
From Proteopedia
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| - | [[Image:2jte.jpg|left|200px]] | + | [[Image:2jte.jpg|left|200px]] |
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| - | '''Third SH3 domain of CD2AP''' | + | {{Structure |
| + | |PDB= 2jte |SIZE=350|CAPTION= <scene name='initialview01'>2jte</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Cd2ap, Mets1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Third SH3 domain of CD2AP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JTE is a [ | + | 2JTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTE OCA]. |
==Reference== | ==Reference== | ||
| - | The high resolution NMR structure of the third SH3 domain of CD2AP., Ortega Roldan JL, Romero Romero ML, Ora A, Ab E, Lopez Mayorga O, Azuaga AI, van Nuland NA, J Biomol NMR. 2007 Dec;39(4):331-6. Epub 2007 Oct 9. PMID:[http:// | + | The high resolution NMR structure of the third SH3 domain of CD2AP., Ortega Roldan JL, Romero Romero ML, Ora A, Ab E, Lopez Mayorga O, Azuaga AI, van Nuland NA, J Biomol NMR. 2007 Dec;39(4):331-6. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17922258 17922258] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''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 17:44:56 2008'' |
Revision as of 15:44, 20 March 2008
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| Gene: | Cd2ap, Mets1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Third SH3 domain of CD2AP
Overview
CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. CD2AP interacts, as an adaptor protein, with different natural targets, such as CD2, nefrin, c-Cbl and podocin. These proteins are believed to interact to one of the three SH3 domains that are positioned in the N-terminal region of CD2AP. To understand the network of interactions between the natural targets and the three SH3 domains (SH3-A, B and C), we have started to determine the structures of the individual SH3 domains. Here we present the high-resolution structure of the SH3-C domain derived from NMR data. Full backbone and side-chain assignments were obtained from triple-resonance spectra. The structure was determined from distance restraints derived from high-resolution 600 and 800 MHz NOESY spectra, together with phi and psi torsion angle restraints based on the analysis of 1HN, 15N, 1Halpha, 13Calpha, 13CO and 13Cbeta chemical shifts. Structures were calculated using CYANA and refined in water using RECOORD. The three-dimensional structure of CD2AP SH3-C contains all the features that are typically found in other SH3 domains, including the general binding site for the recognition of polyproline sequences.
About this Structure
2JTE is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The high resolution NMR structure of the third SH3 domain of CD2AP., Ortega Roldan JL, Romero Romero ML, Ora A, Ab E, Lopez Mayorga O, Azuaga AI, van Nuland NA, J Biomol NMR. 2007 Dec;39(4):331-6. Epub 2007 Oct 9. PMID:17922258
Page seeded by OCA on Thu Mar 20 17:44:56 2008
