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2l5s
From Proteopedia
(Difference between revisions)
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| - | + | [[Image:2l5s.png|left|200px]] | |
| - | The | + | <!-- |
| + | The line below this paragraph, containing "STRUCTURE_2l5s", creates the "Structure Box" on the page. | ||
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| + | {{STRUCTURE_2l5s| PDB=2l5s | SCENE= }} | ||
| - | + | ===Solution structure of the extracellular domain of the TGF-beta type I receptor=== | |
| - | Description: Solution structure of the extracellular domain of the TGF-beta type I receptor | ||
| - | + | <!-- | |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_21821041}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 21821041 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_21821041}} | ||
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| + | ==About this Structure== | ||
| + | [[2l5s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5S OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:021821041</ref><references group="xtra"/> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Receptor protein serine/threonine kinase]] | ||
| + | [[Category: Hinck, C.]] | ||
| + | [[Category: Huang, T.]] | ||
| + | [[Category: Ilangovan, U.]] | ||
| + | [[Category: Pardeep, M.]] | ||
| + | [[Category: Zuniga, J E.]] | ||
| + | [[Category: Alk5]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Transforming growth factor beta]] | ||
| + | [[Category: Type i receptor]] | ||
Revision as of 09:16, 30 October 2011
Solution structure of the extracellular domain of the TGF-beta type I receptor
Template:ABSTRACT PUBMED 21821041
About this Structure
2l5s is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Zuniga JE, Ilangovan U, Mahlawat P, Hinck CS, Huang T, Groppe JC, McEwen DG, Hinck AP. The TbetaR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding. J Mol Biol. 2011 Sep 30;412(4):601-18. Epub 2011 Jul 29. PMID:21821041 doi:10.1016/j.jmb.2011.07.046
