1cf0
From Proteopedia
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| - | [[Image:1cf0.gif|left|200px]] | + | [[Image:1cf0.gif|left|200px]] |
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| - | '''HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE''' | + | {{Structure |
| + | |PDB= 1cf0 |SIZE=350|CAPTION= <scene name='initialview01'>1cf0</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CF0 is a [ | + | 1CF0 is a [[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=1CF0 OCA]. |
==Reference== | ==Reference== | ||
| - | Profilin binds proline-rich ligands in two distinct amide backbone orientations., Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC, Nat Struct Biol. 1999 Jul;6(7):666-71. PMID:[http:// | + | Profilin binds proline-rich ligands in two distinct amide backbone orientations., Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC, Nat Struct Biol. 1999 Jul;6(7):666-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10404225 10404225] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: profilin]] | [[Category: profilin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:32 2008'' |
Revision as of 08:23, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE
Overview
The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.
About this Structure
1CF0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Profilin binds proline-rich ligands in two distinct amide backbone orientations., Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC, Nat Struct Biol. 1999 Jul;6(7):666-71. PMID:10404225
Page seeded by OCA on Thu Mar 20 10:23:32 2008
