1l3h
From Proteopedia
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| - | [[Image:1l3h.jpg|left|200px]] | + | [[Image:1l3h.jpg|left|200px]] |
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| - | '''NMR structure of P41icf, a potent inhibitor of human cathepsin L''' | + | {{Structure |
| + | |PDB= 1l3h |SIZE=350|CAPTION= <scene name='initialview01'>1l3h</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR structure of P41icf, a potent inhibitor of human cathepsin L''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L3H is a [ | + | 1L3H is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12568610 12568610] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barthe, P.]] | [[Category: Barthe, P.]] | ||
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[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
| - | [[Category: disulfide | + | [[Category: disulfide bond]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:49 2008'' |
Revision as of 10:25, 20 March 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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