1t1q
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
- | [[1t1q]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1Q OCA]. | + | [[1t1q]] is a 2 chain structure of [[Molecular Playground/Insulin]]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1Q OCA]. |
+ | |||
+ | ==See Also== | ||
+ | *[[Molecular Playground/Insulin]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015276842</ref><ref group="xtra">PMID:011123908</ref><ref group="xtra">PMID:009148904</ref><ref group="xtra">PMID:008876979</ref><ref group="xtra">PMID:008448120</ref><ref group="xtra">PMID:007014485</ref><references group="xtra"/> |
[[Category: Chu, Y C.]] | [[Category: Chu, Y C.]] | ||
[[Category: Hu, S Q.]] | [[Category: Hu, S Q.]] | ||
Line 34: | Line 37: | ||
[[Category: Xu, B.]] | [[Category: Xu, B.]] | ||
[[Category: Aba-b12-dkp-insulin]] | [[Category: Aba-b12-dkp-insulin]] | ||
- | [[Category: Hormone | + | [[Category: Hormone-growth factor complex]] |
[[Category: Insulin receptor]] | [[Category: Insulin receptor]] | ||
[[Category: Protein unfolding]] | [[Category: Protein unfolding]] | ||
[[Category: Receptor binding]] | [[Category: Receptor binding]] |
Revision as of 06:52, 28 March 2012
Contents |
NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B10-ASP, VAL-B12-ABA, PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES
Template:ABSTRACT PUBMED 15276842
About this Structure
1t1q is a 2 chain structure of Molecular Playground/Insulin. Full experimental information is available from OCA.
See Also
Reference
- Huang K, Xu B, Hu SQ, Chu YC, Hua QX, Qu Y, Li B, Wang S, Wang RY, Nakagawa SH, Theede AM, Whittaker J, De Meyts P, Katsoyannis PG, Weiss MA. How insulin binds: the B-chain alpha-helix contacts the L1 beta-helix of the insulin receptor. J Mol Biol. 2004 Aug 6;341(2):529-50. PMID:15276842 doi:10.1016/j.jmb.2004.05.023
- Nakagawa SH, Tager HS, Steiner DF. Mutational analysis of invariant valine B12 in insulin: implications for receptor binding. Biochemistry. 2000 Dec 26;39(51):15826-35. PMID:11123908
- Kristensen C, Kjeldsen T, Wiberg FC, Schaffer L, Hach M, Havelund S, Bass J, Steiner DF, Andersen AS. Alanine scanning mutagenesis of insulin. J Biol Chem. 1997 May 16;272(20):12978-83. PMID:9148904
- Wang QQ, Feng YM, Zhang YS. Studies on receptor binding site of insulin: the hydrophobic B12Val can be substituted by hydrophilic thr. Biochem Mol Biol Int. 1996 Aug;39(6):1245-54. PMID:8876979
- Hu SQ, Burke GT, Schwartz GP, Ferderigos N, Ross JB, Katsoyannis PG. Steric requirements at position B12 for high biological activity in insulin. Biochemistry. 1993 Mar 16;32(10):2631-5. PMID:8448120
- Schwartz GP, Burke GT, Katsoyannis PG. [12-asparagine-B] human insulin. An analogue with modification in the hydrophobic core of insulin. Int J Pept Protein Res. 1981 Feb;17(2):243-55. PMID:7014485