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1g9e

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{{STRUCTURE_1g9e| PDB=1g9e | SCENE= }}
{{STRUCTURE_1g9e| PDB=1g9e | SCENE= }}
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'''SOLUTION STRUCTURE AND RELAXATION MEASUREMENTS OF AN ANTIGEN-FREE HEAVY CHAIN VARIABLE DOMAIN (VHH) FROM LLAMA'''
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===SOLUTION STRUCTURE AND RELAXATION MEASUREMENTS OF AN ANTIGEN-FREE HEAVY CHAIN VARIABLE DOMAIN (VHH) FROM LLAMA===
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==Overview==
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Camelids, (dromedaries, camels, and llamas) produce heavy-chains antibodies, with their antigen recognition sites composed of a single VH-like domain, referred to as VHH. The solution structure of one of these VHHs domains (VHH-H14), raised against the alpha subunit of the human chorionic gonadotropin hormone (hCG), has been determined by (15)N heteronuclear three-dimensional NMR spectroscopy. The framework is well resolved within the set of 20 best-calculated NMR structures and is close to that of classical VH domains from vertebrate antibodies, consisting of two antiparallel beta-sheets organized in a beta-barrel. Loops display a lower precision, especially the Complementarity Determining Regions (CDRs), involved in antigen recognition. Comparison of the three-dimensional VHH-H14 solution structure with its previously solved crystal structure (Spinelli et al., Nature Struct. Biol. 1996;3:752-757) reveals a high similarity to the framework, whereas significant conformational differences occur on CDRs, leading to the assumption that the antigen recognition site is a more mobile part. In order to deepen our insights into the dynamics of VHH-H14 in solution, (15)N relaxation was measured with longitudinal R1 and transverse R2 self-relaxation rates, and (15)N steady-state heteronuclear nuclear Overhauser enhancements (NOE), making it possible to probe picosecond-to-millisecond internal motions. Determination of dynamic parameters (S(2), tau(e), and Rex) through the Lipari-Szabo Model-free approach enables the identification of several regions with enhanced dynamics. Especially, the mobility measurements from NMR confirm that the antigen recognition site is the most mobile part of the VHH-H14 domain on picosecond-to-nanosecond fast time scales. Several residues belonging to the three CDRs are submitted to chemical exchange processes occurring on slow microsecond-to-millisecond time scales, suggesting that the formation of the VHH/antigen complex should be accompanied by structural changes.
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{{ABSTRACT_PUBMED_12001233}}
==About this Structure==
==About this Structure==
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1G9E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G9E OCA].
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1G9E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G9E OCA].
==Reference==
==Reference==
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[[Category: Renisio, J G.]]
[[Category: Renisio, J G.]]
[[Category: Beta barrel]]
[[Category: Beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:56:18 2008''

Revision as of 01:56, 1 July 2008

Image:1g9e.png

Template:STRUCTURE 1g9e

SOLUTION STRUCTURE AND RELAXATION MEASUREMENTS OF AN ANTIGEN-FREE HEAVY CHAIN VARIABLE DOMAIN (VHH) FROM LLAMA

Template:ABSTRACT PUBMED 12001233

About this Structure

1G9E is a Single protein structure of sequence from Lama glama. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from Llama., Renisio JG, Perez J, Czisch M, Guenneugues M, Bornet O, Frenken L, Cambillau C, Darbon H, Proteins. 2002 Jun 1;47(4):546-55. PMID:12001233

Page seeded by OCA on Tue Jul 1 04:56:18 2008

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