|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1-3
|
|
pubmed:dateCreated |
2002-8-6
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The Rnd proteins constitute an exceptional subfamily within the Rho GTPase family. They possess extended chains at both termini and four prominent amino acid deviations causing GTPase deficiency. Herein, we report the crystal structure of the Rnd3/RhoE G-domain (amino acids 19-200) at 2.0 A resolution. This is the first GTP-structure of a Rho family member which reveals a similar fold but striking differences from RhoA concerning (i) GTPase center, (ii) charge distribution at several surface areas, (iii) C3-transferase binding site and (iv) interacting interfaces towards RhoA regulators and effectors.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Botulinum Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/RND3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/exoenzyme C3, Clostridium botulinum,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTPase-activating protein,
http://linkedlifedata.com/resource/pubmed/chemical/rho guanine nucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/rho guanine nucleotide exchange...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
525
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
100-4
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:12163169-ADP Ribose Transferases,
pubmed-meshheading:12163169-Binding Sites,
pubmed-meshheading:12163169-Botulinum Toxins,
pubmed-meshheading:12163169-Crystallography, X-Ray,
pubmed-meshheading:12163169-GTPase-Activating Proteins,
pubmed-meshheading:12163169-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:12163169-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:12163169-Guanosine Triphosphate,
pubmed-meshheading:12163169-Humans,
pubmed-meshheading:12163169-Models, Molecular,
pubmed-meshheading:12163169-Molecular Sequence Data,
pubmed-meshheading:12163169-Protein Binding,
pubmed-meshheading:12163169-Protein Structure, Tertiary,
pubmed-meshheading:12163169-Sequence Homology, Amino Acid,
pubmed-meshheading:12163169-Structure-Activity Relationship,
pubmed-meshheading:12163169-rho GTP-Binding Proteins
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
Crystal structure of Rnd3/RhoE: functional implications.
|
|
pubmed:affiliation |
Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
