1tta

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[[Image:1tta.png|left|200px]]
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{{STRUCTURE_1tta| PDB=1tta | SCENE= }}
{{STRUCTURE_1tta| PDB=1tta | SCENE= }}
===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==
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1TTA is a 2 chains structure of sequences 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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[[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==
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*[[Transthyretin|Transthyretin]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8428915</ref><references group="xtra"/>
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<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

Image:1tta.png

Template:STRUCTURE 1tta

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

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