spacer
spacer

PDBsum entry 1jtt

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Immune system, lysozyme PDB id
1jtt
Contents
Protein chains
133 a.a. *
129 a.a. *
Ligands
FMT ×9
Metals
_NA ×6
Waters ×213
* Residue conservation analysis

References listed in PDB file
Key reference
Title Degenerate interfaces in antigen-Antibody complexes.
Authors K.Decanniere, T.R.Transue, A.Desmyter, D.Maes, S.Muyldermans, L.Wyns.
Ref. J Mol Biol, 2001, 313, 473-478. [DOI no: 10.1006/jmbi.2001.5075]
PubMed id 11676532
Abstract
In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.
Figure 1.
Figure 1. Superposition of the hel1 and hel2 com- plexes: (a) using all main-chain atoms; (b) using main- chain atoms of cAb-Lys3 only; (c) superposition as in (b), comparing the hel1 complex with the hel-C2 com- plex; (d) superposition as in (b), comparing the tel1 and tel2 complexes. cAb-Lys3 molecules are in grey and dark green, lysozyme is in yellow and blue.
Figure 2.
Figure 2. Differences in (a) buried surface area and (b) Voronoi volume for the cAb-Lys3 interface atoms between the hel1 and hel2 complex. Dark colours rep- resent little or no change, light colours represent large differences. CDR1 atoms are coloured blue, CDR2 atoms are yellow, and the CDR3 atoms are red. Green halos around CDR3 atoms indicate atoms making hydrogen bonds with the antigen. Framework atoms are grey.
The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 313, 473-478) copyright 2001.
Secondary reference #1
Title Crystal structure of a camel single-Domain vh antibody fragment in complex with lysozyme.
Authors A.Desmyter, T.R.Transue, M.A.Ghahroudi, M.H.Thi, F.Poortmans, R.Hamers, S.Muyldermans, L.Wyns.
Ref. Nat Struct Biol, 1996, 3, 803-811.
PubMed id 8784355
Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer