From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ieh.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ieh.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ieh| PDB=1ieh | SCENE= }} | | {{STRUCTURE_1ieh| PDB=1ieh | SCENE= }} |
| | | | |
| - | '''SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE'''
| + | ===SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The three-dimensional structure of a llama single-domain antibody BrucD4-4 was established by use of solution NMR spectroscopy. BrucD4-4 has Val, Gly, Leu, and Trp residues at positions 37, 44, 45, and 47, which are considered to be a hallmark to distinguish llama VH from V(H)H fragments at the germline level. In contrast to the murine and human VHs, BrucD4-4 has sufficient solubility, is monomeric in solution, and displays high-quality NMR spectra characteristic of well-structured proteins. Amide proton/deuterium exchange and the (15)N relaxation data showed that BrucD4-4 has a classic protein structure with a well-packed core and comparatively mobile surface loops. The three-dimensional architecture of BrucD4-4 is analogous to that of VHs from murine and human F(v)s and camelid V(H)Hs with two pleated beta-sheets formed by four and five beta-strands. A canonical and undistorted beta-barrel exposes a number of hydrophobic residues into the solvent on the surface of the three-dimensional structure. The eight-residue H3 loop folds over the side chain of Val37 similarly to that in llama V(H)Hs; however, this interaction may be transient due to the H3 conformational flexibility. Overall, the surface characteristics of BrucD4-4 with respect to hydrophobicity appear to lie between the human VH domain from Fv Pot and the llama V(H)H fragment HC-V, which may explain its enhanced solubility allowing NMR structural analysis. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12093273}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12093273 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12093273}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEH OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEH OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 29: |
Line 33: |
| | [[Category: Immunoglobulin beta-barrel]] | | [[Category: Immunoglobulin beta-barrel]] |
| | [[Category: Two pleated beta-sheet]] | | [[Category: Two pleated beta-sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:54:43 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:50:47 2008'' |
Revision as of 07:50, 1 July 2008
Template:STRUCTURE 1ieh
SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE
Template:ABSTRACT PUBMED 12093273
About this Structure
Full experimental information is available from OCA.
Reference
Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface., Vranken W, Tolkatchev D, Xu P, Tanha J, Chen Z, Narang S, Ni F, Biochemistry. 2002 Jul 9;41(27):8570-9. PMID:12093273
Page seeded by OCA on Tue Jul 1 10:50:47 2008
