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1tta
From Proteopedia
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===THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION=== | ===THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION=== | ||
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{{ABSTRACT_PUBMED_8428915}} | {{ABSTRACT_PUBMED_8428915}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1tta]] is a 2 chain structure of [[Transthyretin]] with 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=1TTA OCA]. | |
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| + | ==See Also== | ||
| + | *[[Transthyretin|Transthyretin]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008428915</ref><ref group="xtra">PMID:011734033</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Braden, B C.]] | [[Category: Braden, B C.]] | ||
[[Category: Hamilton, J A.]] | [[Category: Hamilton, J A.]] | ||
[[Category: Steinrauf, L K.]] | [[Category: Steinrauf, L K.]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:44:29 2009'' | ||
Revision as of 05:36, 27 July 2012
Contents |
THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8428915
About this Structure
1tta is a 2 chain structure of Transthyretin with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L. The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J Biol Chem. 1993 Feb 5;268(4):2416-24. PMID:8428915
- Sharman GJ, Griffiths-Jones SR, Jourdan M, Searle MS. Effects of amino acid phi,psi propensities and secondary structure interactions in modulating H alpha chemical shifts in peptide and protein beta-sheet. J Am Chem Soc. 2001 Dec 12;123(49):12318-24. PMID:11734033
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
