1htj
From Proteopedia
(New page: 200px<br /> <applet load="1htj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1htj, resolution 2.2Å" /> '''STRUCTURE OF THE RGS...) |
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caption="1htj, resolution 2.2Å" /> | caption="1htj, resolution 2.2Å" /> | ||
'''STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF'''<br /> | '''STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1HTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rgs-like]] | [[Category: rgs-like]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:58:03 2008'' |
Revision as of 13:58, 15 February 2008
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STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF
Overview
BACKGROUND: The multidomain PDZ-RhoGEF is one of many known guanine, nucleotide exchange factors that upregulate Rho GTPases. PDZ-RhoGEF and, related family members play a critical role in a molecular signaling, pathway from heterotrimeric G protein-coupled receptors to Rho proteins. A, approximately 200 residue RGS-like (RGSL) domain in PDZ-RhoGEF and its, homologs is responsible for the direct association with Galpha12/13, proteins. To better understand structure-function relationships, we, initiated crystallographic studies of the RGSL domain from human, PDZ-RhoGEF. RESULTS: A recombinant construct of the RGSL domain was, expressed in Escherichia coli and purified, but it did not crystallize., Alternative constructs were designed based on a novel strategy of, targeting lysine and glutamic acid residues for mutagenesis to alanine. A, triple-point mutant functionally identical to the wild-type protein was, crystallized, and its structure was determined by the MAD method using, Se-methionine (Se-Met) incorporation. A molecular model of the RGSL domain, was refined at 2.2 A resolution, revealing an all-helical tertiary fold, with the mutations located at intermolecular lattice contacts., CONCLUSIONS: The first nine helices adopt a fold similar to that observed, for RGS proteins, although the sequence identity with other such known, structures is below 20%. The last three helices are an integral extension, of the RGS fold, packing tightly against helices 3 and 4 with multiple, hydrophobic interactions. Comparison with RGS proteins suggests features, that are likely relevant for interaction with G proteins. Finally, we, conclude that the strategy used to produce crystals was beneficial and, might be applicable to other proteins resistant to crystallization.
About this Structure
1HTJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases., Longenecker KL, Lewis ME, Chikumi H, Gutkind JS, Derewenda ZS, Structure. 2001 Jul 3;9(7):559-69. PMID:11470431
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