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| - | [[Image:1u2h.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1u2h| PDB=1u2h | SCENE= }} | | {{STRUCTURE_1u2h| PDB=1u2h | SCENE= }} |
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| - | '''X-ray Structure of the N-terminally truncated human APEP-1'''
| + | ===X-ray Structure of the N-terminally truncated human APEP-1=== |
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| - | ==Overview==
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| - | BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16354304}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16354304 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16354304}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rgd motif]] | | [[Category: Rgd motif]] |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:40:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:57:21 2008'' |
Revision as of 21:57, 5 July 2008
Template:STRUCTURE 1u2h
X-ray Structure of the N-terminally truncated human APEP-1
Template:ABSTRACT PUBMED 16354304
About this Structure
1U2H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1)., Manjasetty BA, Niesen FH, Scheich C, Roske Y, Goetz F, Behlke J, Sievert V, Heinemann U, Bussow K, BMC Struct Biol. 2005 Dec 14;5:21. PMID:16354304
Page seeded by OCA on Sun Jul 6 00:57:21 2008
