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| | {{STRUCTURE_1ro3| PDB=1ro3 | SCENE= }} | | {{STRUCTURE_1ro3| PDB=1ro3 | SCENE= }} |
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| - | '''New structural insights on short disintegrin echistatin by NMR'''
| + | ===New structural insights on short disintegrin echistatin by NMR=== |
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| - | ==Overview==
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| - | Echistatin is a potent antagonist of the integrins alpha(v)beta3, alpha5beta1 and alpha(IIb)beta3. Its full inhibitory activity depends on an RGD (Arg-Gly-Asp) motif expressed at the tip of the integrin-binding loop and on its C-terminal tail. Previous NMR structures of echistatin showed a poorly defined integrin-recognition sequence and an incomplete C-terminal tail, which left the molecular basis of the functional synergy between the RGD loop and the C-terminal region unresolved. We report a high-resolution structure of echistatin and an analysis of its internal motions by off-resonance ROESY (rotating-frame Overhauser enhancement spectroscopy). The full-length C-terminal polypeptide is visible as a beta-hairpin running parallel to the RGD loop and exposing at the tip residues Pro43, His44 and Lys45. The side chains of the amino acids of the RGD motif have well-defined conformations. The integrin-binding loop displays an overall movement with maximal amplitude of 30 degrees . Internal angular motions in the 100-300 ps timescale indicate increased flexibility for the backbone atoms at the base of the integrin-recognition loop. In addition, backbone atoms of the amino acids Ala23 (flanking the R24GD26 tripeptide) and Asp26 of the integrin-binding motif showed increased angular mobility, suggesting the existence of major and minor hinge effects at the base and the tip, respectively, of the RGD loop. A strong network of NOEs (nuclear Overhauser effects) between residues of the RGD loop and the C-terminal tail indicate concerted motions between these two functional regions. A full-length echistatin-alpha(v)beta3 docking model suggests that echistatin's C-terminal amino acids may contact alpha(v)-subunit residues and provides new insights to delineate structure-function correlations.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15535803}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15535803 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15535803}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1RO3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Echis_carinatus Echis carinatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO3 OCA]. | + | 1RO3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Echis_carinatus Echis carinatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO3 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Monleon, D.]] | | [[Category: Monleon, D.]] |
| | [[Category: No regular secondary structure]] | | [[Category: No regular secondary structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:43:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:59:48 2008'' |
Revision as of 08:59, 28 July 2008
Template:STRUCTURE 1ro3
New structural insights on short disintegrin echistatin by NMR
Template:ABSTRACT PUBMED 15535803
About this Structure
1RO3 is a Single protein structure of sequence from Echis carinatus. Full experimental information is available from OCA.
Reference
Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR., Monleon D, Esteve V, Kovacs H, Calvete JJ, Celda B, Biochem J. 2005 Apr 1;387(Pt 1):57-66. PMID:15535803
Page seeded by OCA on Mon Jul 28 11:59:48 2008
