Abstract
So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amine acid sequence. Here, we analyse the conformation of this loop and show that we life able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues ban also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 9-16 |
| Number of pages | 8 |
| Journal | Biophysical Chemistry |
| Volume | 68 |
| Issue number | 1-3 |
| DOIs | |
| State | Published - Oct 1 1997 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Organic Chemistry
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Antibody structure, prediction and redesign. / Morea, V.; Tramontano, A.; Rustici, M.; Chothia, C.; Lesk, Arthur.
In: Biophysical Chemistry, Vol. 68, No. 1-3, 01.10.1997, p. 9-16.Research output: Contribution to journal › Article
TY - JOUR
T1 - Antibody structure, prediction and redesign
AU - Morea, V.
AU - Tramontano, A.
AU - Rustici, M.
AU - Chothia, C.
AU - Lesk, Arthur
PY - 1997/10/1
Y1 - 1997/10/1
N2 - So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amine acid sequence. Here, we analyse the conformation of this loop and show that we life able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues ban also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.
AB - So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amine acid sequence. Here, we analyse the conformation of this loop and show that we life able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues ban also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.
UR - http://www.scopus.com/inward/record.url?scp=0031405336&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031405336&partnerID=8YFLogxK
U2 - 10.1016/S0301-4622(96)02266-1
DO - 10.1016/S0301-4622(96)02266-1
M3 - Article
C2 - 9468606
AN - SCOPUS:0031405336
VL - 68
SP - 9
EP - 16
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 1-3
ER -