1qac
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1qac.gif|left|200px]] | [[Image:1qac.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1qac", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1qac| PDB=1qac | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE''' | '''CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAC OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11045631 11045631] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11045631 11045631] | ||
| - | [[Category: Homo sapiens]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Cai, X.]] | [[Category: Cai, X.]] | ||
[[Category: Johnson, G.]] | [[Category: Johnson, G.]] | ||
| Line 30: | Line 25: | ||
[[Category: Schiffer, M.]] | [[Category: Schiffer, M.]] | ||
[[Category: Stevens, F J.]] | [[Category: Stevens, F J.]] | ||
| - | [[Category: | + | [[Category: Beta barrel immunoglobulin vl domain dimer]] |
| - | [[Category: | + | [[Category: Flipped domain dimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:03:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:03, 3 May 2008
CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE
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
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 Page seeded by OCA on Sat May 3 06:03:45 2008
