1uik: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1uik.jpg|left|200px]]
{{Seed}}
[[Image:1uik.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uik|  PDB=1uik  |  SCENE=  }}  
{{STRUCTURE_1uik|  PDB=1uik  |  SCENE=  }}  


'''Crystal structure of soybean beta-conglycinin alpha prime homotrimer'''
===Crystal structure of soybean beta-conglycinin alpha prime homotrimer===




==Overview==
<!--
The crystal structure of the core region of the alpha' subunit (alpha(c')) of soybean beta-conglycinin has been determined at 2.3 A resolution. alpha(c') was superimposed on the known crystal structure of the beta-conglycinin beta subunit with a small root-mean square deviation of 0.77 A, which is consistent with the high sequence identity of 75.5% between alpha(c') and the beta subunit. It is known that the thermal stability of the beta subunit is higher than that of the alpha' subunit and that their thermal stabilities are conferred by highly homologous core regions. Comparisons of the three-dimensional structures and primary sequences between alpha(c') and the beta subunit suggest that five factors account for this difference between subunits as regards the difference in thermal stability: (i) the total cavity volume is larger in alpha(c'), (ii) the cluster of charged residues at the intermonomer interface is smaller in alpha(c') and alpha(c') lacks the intermonomer salt bridge of the beta subunit, (iii) the solvent-accessible surface is more hydrophobic in alpha(c'), (iv) there are fewer proline residues in alpha(c') and (v) a loop region between helix 3 and strand J' in alpha(c') is more flexible owing to the insertion of five additional residues. Although more hydrogen bonds were found in alpha(c'), this difference should be more than compensated for by the combined contributions of these other factors.
The line below this paragraph, {{ABSTRACT_PUBMED_14747705}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14747705 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14747705}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Utsumi, S.]]
[[Category: Utsumi, S.]]
[[Category: Double-stranded beta-helix]]
[[Category: Double-stranded beta-helix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:16:50 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:07:15 2008''

Revision as of 17:07, 28 July 2008

File:1uik.png

Template:STRUCTURE 1uik

Crystal structure of soybean beta-conglycinin alpha prime homotrimer

Template:ABSTRACT PUBMED 14747705

About this Structure

1UIK is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Structure of the core region of the soybean beta-conglycinin alpha' subunit., Maruyama Y, Maruyama N, Mikami B, Utsumi S, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):289-97. Epub 2004, Jan 23. PMID:14747705

Page seeded by OCA on Mon Jul 28 20:07:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1uik&oldid=713459"