1mr3: Difference between revisions

[[Image:1mr3.gif|left|200px]]<br /><applet load="1mr3" size="350" color="white" frame="true" align="right" spinBox="true"  

Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with previously determined structures of human ARF1 and ARF6. These analyses revealed an overall conserved fold but differences in primary sequence and length, particularly in an N-terminal loop, lead to differences in nucleotide and divalent metal binding. Packing of hydrophobic residues is central to the interplay between the N-terminal alpha-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins.

1MR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=G3D:'>G3D</scene>, <scene name='pdbligand=EDO:'>EDO</scene>, <scene name='pdbligand=GOL:'>GOL</scene>, <scene name='pdbligand=EOH:'>EOH</scene> and <scene name='pdbligand=PDO:'>PDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR3 OCA].  

[[Category: Amor, J C.]]

[[Category: Horton, J R.]]

[[Category: Kahn, R A.]]

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