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1fsb

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{{STRUCTURE_1fsb| PDB=1fsb | SCENE= }}
{{STRUCTURE_1fsb| PDB=1fsb | SCENE= }}
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'''STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES'''
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===STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES===
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==Overview==
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P-selectin is a multidomain adhesion protein on the surface of activated platelets and endothelial cells that functions in the recruitment of leukocytes to the site of inflammation. The amino-terminal lectin and EGF domains constitute the ligand recognition unit. We have produced a synthetic 40-residue P-selectin EGF domain (P-sel:EGF) to examine the structure and function of this domain independent of P-selectin. The peptide was folded in vitro and exhibited the same disulfide bonding pattern as other EGF-like domains. P-sel:EGF did not inhibit P-selectin-mediated cellular adhesion assays, indicating that the lectin domain is also required. We undertook the study of the P-selectin EGF by 1H NMR to determine its structure independent of the lectin domain and to compare its structure to that of E-selectin determined crystallographically [Graves et al. (1994) Nature 367, 532]. Although the binding of P-selectin to its carbohydrate ligand is calcium dependent, and some EGF domains have calcium binding sites, addition of calcium had no effect on the NMR spectrum or on the pH-induced changes. Nearly complete resonance assignments were made from 2D 1H NMR spectra at pH 6.0. Two sections of antiparallel beta-sheet were identified on the basis of the pattern of long-range NOEs, 3JHN alpha coupling constants, and slowly exchanging amides. The solution structure of the peptide backbone was determined using distance geometry and simulated annealing calculations. The backbone RMSD to the geometric average for 19 final structures is 0.64 +/- 0.17 A. The resulting fold closely resembles that of other EGF-like peptides, including the E-selectin EGF domain (RMSD approximately 1.08 A). However, compared to the E-selectin EGF structure which also contains the lectin domain, some residues from 1-11 are less ordered, and novel contacts occur between the amino terminus and the core beta-sheet. Despite marked structural homology of the selectin polypeptide backbones, the selectin EGF surfaces show unique distributions of charged residues, a feature that likely correlates to the functional differences.
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{{ABSTRACT_PUBMED_8901515}}
==About this Structure==
==About this Structure==
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1FSB 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=1FSB OCA].
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1FSB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSB OCA].
==Reference==
==Reference==
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[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:42:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:52:21 2008''

Revision as of 00:52, 1 July 2008

Image:1fsb.png

Template:STRUCTURE 1fsb

STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES

Template:ABSTRACT PUBMED 8901515

About this Structure

1FSB is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structure and function of the epidermal growth factor domain of P-selectin., Freedman SJ, Sanford DG, Bachovchin WW, Furie BC, Baleja JD, Furie B, Biochemistry. 1996 Oct 29;35(43):13733-44. PMID:8901515

Page seeded by OCA on Tue Jul 1 03:52:21 2008

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