5lve
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(New page: 200px<br /><applet load="5lve" size="450" color="white" frame="true" align="right" spinBox="true" caption="5lve, resolution 2.00Å" /> '''STRUCTURE OF THE VAR...)
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Revision as of 17:28, 20 November 2007
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STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN
Overview
The importance of unsatisfied hydrogen bonding potential on, protein-protein interaction was studied. Two alternate modes of, dimerization (conventional and flipped form) of an immunoglobulin light, chain variable domain (V(L)) were previously identified. In the flipped, form, interface residue Gln89 would have an unsatisfied hydrogen bonding, potential. Removal of this Gln should render the flipped dimer as the more, favorable quaternary form. High resolution crystallographic studies of the, Q89A and Q89L mutants show, as we predicted, that these proteins indeed, form flipped dimers with very similar interfaces. A small cavity is, present in the Q89A mutant that is reflected in the approximately 100, times lower association constant than found for the Q89L mutant. The, association constant of Q89A and Q89L proteins (4 x 10(6) M(-1) and >10(8), M(-1)) are 10- and 1,000-fold higher than that of the wild-type protein, that forms conventional dimers clearly showing the energetic reasons for, the flipped dimer formation.
About this Structure
5LVE is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface., Pokkuluri PR, Cai X, Johnson G, Stevens FJ, Schiffer M, Protein Sci. 2000 Sep;9(9):1852-5. PMID:11045631
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