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PDBsum entry 1jwu

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Top Page protein Protein-protein interface(s) links
Immune system PDB id
1jwu
Jmol
Contents
Protein chains
180 a.a. *
187 a.a. *
13 a.a. *
232 a.a. *
Waters ×178
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structural, Energetic, And functional analysis of a protein-Protein interface at distinct stages of affinity maturation.
Authors E.J.Sundberg, P.S.Andersen, P.M.Schlievert, K.Karjalainen, R.A.Mariuzza.
Ref. Structure, 2003, 11, 1151-1161. [DOI no: 10.1016/S0969-2126(03)00187-4]
PubMed id 12962633
Abstract
Due to a paucity of studies that synthesize structural, energetic, and functional analyses of a series of protein complexes representing distinct stages in an affinity maturation pathway, the biophysical basis for the molecular evolution of protein-protein interactions is poorly understood. Here, we combine crystal structures and binding-free energies of a series of variant superantigen (SAG)-major histocompatibility complex (MHC) class II complexes exhibiting increasingly higher affinity to reveal that this affinity maturation pathway is controlled largely by two biophysical factors: shape complementarity and buried hydrophobic surface. These factors, however, do not contribute equivalently to the affinity maturation of the interface, as the former dominates the early steps of the maturation process while the latter is responsible for improved binding in later steps. Functional assays reveal how affinity maturation of the SAG-MHC interface corresponds to T cell activation by SAGs.
Figure 1.
Figure 1. Structural Validation of the Wild-Type and Mutant SEC3-DR1 ComplexesStereodiagrams of composite annealed omit electron density maps in the variant region (residues 43-47) of (A) SEC3-wt, (B) SEC3-3B1, and (C) SEC3-3B2. All electron density maps are contoured at 1.4s. Figure produced using Bobscript (Esnouf, 1997) and Raster3D (Merritt and Bacon, 1997).
The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1151-1161) copyright 2003.
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