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1qac

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[[Image:1qac.gif|left|200px]]
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{{STRUCTURE_1qac| PDB=1qac | SCENE= }}
{{STRUCTURE_1qac| PDB=1qac | SCENE= }}
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'''CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE'''
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===CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE===
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==Overview==
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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 &gt;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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11045631}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11045631 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11045631}}
==About this Structure==
==About this Structure==
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[[Category: Beta barrel immunoglobulin vl domain dimer]]
[[Category: Beta barrel immunoglobulin vl domain dimer]]
[[Category: Flipped domain dimer]]
[[Category: Flipped domain dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:03:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:17:39 2008''

Revision as of 06:17, 28 July 2008

Image:1qac.png

Template:STRUCTURE 1qac

CHANGE IN DIMERIZATION MODE BY REMOVAL OF A SINGLE UNSATISFIED POLAR RESIDUE

Template:ABSTRACT PUBMED 11045631

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 Mon Jul 28 09:17:39 2008

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