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| - | [[Image:1d1j.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1d1j| PDB=1d1j | SCENE= }} | | {{STRUCTURE_1d1j| PDB=1d1j | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF HUMAN PROFILIN II'''
| + | ===CRYSTAL STRUCTURE OF HUMAN PROFILIN II=== |
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| - | ==Overview==
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| - | Human profilins are multifunctional, single-domain proteins which directly link the actin microfilament system to a variety of signalling pathways via two spatially distinct binding sites. Profilin binds to monomeric actin in a 1:1 complex, catalyzes the exchange of the actin-bound nucleotide and regulates actin filament barbed end assembly. Like SH3 domains, profilin has a surface-exposed aromatic patch which binds to proline-rich peptides. Various multidomain proteins including members of the Ena/VASP and formin families localize profilin:actin complexes through profilin:poly-L-proline interactions to particular cytoskeletal locations (e.g. focal adhesions, cleavage furrows). Humans express a basic (I) and an acidic (II) isoform of profilin which exhibit different affinities for peptides and proteins rich in proline residues. Here, we report the crystallization and X-ray structure determination of human profilin II to 2.2 A. This structure reveals an aromatic extension of the previously defined poly-L-proline binding site for profilin I. In contrast to serine 29 of profilin I, tyrosine 29 in profilin II is capable of forming an additional stacking interaction and a hydrogen bond with poly-L-proline which may account for the increased affinity of the second isoform for proline-rich peptides. Differential isoform specificity for proline-rich proteins may be attributed to the differences in charged and hydrophobic residues in and proximal to the poly-L-proline binding site. The actin-binding face remains nearly identical with the exception of five amino acid differences. These observations are important for the understanding of the functional and structural differences between these two classes of profilin isoforms.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10600384}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10600384 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10600384}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Actin-binding protein]] | | [[Category: Actin-binding protein]] |
| | [[Category: Poly-l-proline binding protein]] | | [[Category: Poly-l-proline binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:20:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:04:37 2008'' |
Revision as of 19:04, 30 June 2008
Template:STRUCTURE 1d1j
CRYSTAL STRUCTURE OF HUMAN PROFILIN II
Template:ABSTRACT PUBMED 10600384
About this Structure
1D1J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structure determination of human profilin II: A comparative structural analysis of human profilins., Nodelman IM, Bowman GD, Lindberg U, Schutt CE, J Mol Biol. 1999 Dec 17;294(5):1271-85. PMID:10600384
Page seeded by OCA on Mon Jun 30 22:04:37 2008
