1op1: Difference between revisions
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[[Image:1op1.gif|left|200px]] | [[Image:1op1.gif|left|200px]] | ||
'''Solution NMR structure of domain 1 of receptor associated protein''' | {{Structure | ||
|PDB= 1op1 |SIZE=350|CAPTION= <scene name='initialview01'>1op1</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= LRPAP1 OR A2MRAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Solution NMR structure of domain 1 of receptor associated protein''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OP1 is a [ | 1OP1 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=1OP1 OCA]. | ||
==Reference== | ==Reference== | ||
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein., Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX, J Biomol NMR. 2003 Jun;26(2):187-8. PMID:[http:// | 1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein., Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX, J Biomol NMR. 2003 Jun;26(2):187-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12766414 12766414] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical bundle]] | [[Category: helical bundle]] | ||
''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 13:13:42 2008'' | ||
Revision as of 11:13, 20 March 2008
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| Gene: | LRPAP1 OR A2MRAP (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Solution NMR structure of domain 1 of receptor associated protein
Overview
The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.
About this Structure
1OP1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein., Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX, J Biomol NMR. 2003 Jun;26(2):187-8. PMID:12766414
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