5lve: Difference between revisions
New page: left|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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[[Image:5lve.gif|left|200px]]<br /><applet load="5lve" size=" | [[Image:5lve.gif|left|200px]]<br /><applet load="5lve" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="5lve, resolution 2.00Å" /> | caption="5lve, resolution 2.00Å" /> | ||
'''STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN'''<br /> | '''STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN'''<br /> | ||
==Overview== | ==Overview== | ||
The importance of unsatisfied hydrogen bonding potential on | 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== | ==About this Structure== | ||
5LVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 5LVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chang, C | [[Category: Chang, C H.]] | ||
[[Category: Huang, D | [[Category: Huang, D B.]] | ||
[[Category: Schiffer, M.]] | [[Category: Schiffer, M.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:29 2008'' | ||
Revision as of 20:15, 21 February 2008
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STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN
OverviewOverview
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 StructureAbout this Structure
5LVE is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Feb 21 19:15:29 2008