1l3h
From Proteopedia
(New page: 200px<br /> <applet load="1l3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3h" /> '''NMR structure of P41icf, a potent inhibitor...) |
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'''NMR structure of P41icf, a potent inhibitor of human cathepsin L'''<br /> | '''NMR structure of P41icf, a potent inhibitor of human cathepsin L'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1L3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: disulfide bonds]] | [[Category: disulfide bonds]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:16:25 2008'' |
Revision as of 14:16, 15 February 2008
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NMR structure of P41icf, a potent inhibitor of human cathepsin L
Overview
The total synthesis and structural characterization of the, MHCII-associated p41 invariant chain fragment (P41icf) is described., P41icf plays a crucial role in the maturation of MHC class II molecules, and antigen processing, acting as a highly selective cathepsin L, inhibitor. P41icf synthesis was achieved using a combined, solid-phase/solution approach. The entire molecule (65 residues, 7246 Da, unprotected) was assembled in solution from fully protected peptides in, the size range of 10 residues. After deprotection, oxidative folding in, carefully adjusted experimental conditions led to the completely folded, and functional P41icf with a disulfide pairing identical to that of native, P41icf. CD, NMR, and surface plasmon resonance (SPR) were used for the, structural and functional characterization of synthetic P41icf. CD thermal, denaturation showed clear cooperative behavior. Tight cathepsin L binding, was demonstrated by SPR. (1)H NMR spectroscopy at 800 MHz of unlabeled, P41icf was used to solve the three-dimensional structure of the molecule., P41icf behaves as a well-folded protein domain with a topology very close, to the crystallographic cathepsin L-bound form.
About this Structure
1L3H is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Synthesis and NMR structure of p41icf, a potent inhibitor of human cathepsin L., Chiva C, Barthe P, Codina A, Gairi M, Molina F, Granier C, Pugniere M, Inui T, Nishio H, Nishiuchi Y, Kimura T, Sakakibara S, Albericio F, Giralt E, J Am Chem Soc. 2003 Feb 12;125(6):1508-17. PMID:12568610
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