1fsb

<StructureSection load='1fsb' size='340' side='right'caption='[[1fsb]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1fsb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FSB FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsb OCA], [https://pdbe.org/1fsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fsb RCSB], [https://www.ebi.ac.uk/pdbsum/1fsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsb ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/LYAM3_HUMAN LYAM3_HUMAN]] Defects in SELP may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:14681304</ref>

[[https://www.uniprot.org/uniprot/LYAM3_HUMAN LYAM3_HUMAN]] Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1.<ref>PMID:7585950</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8901515</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fsb" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Bachovchin, W W]]

[[Category: Baleja, J D]]

[[Category: Freedman, S J]]

[[Category: Furie, B]]

[[Category: Furie, B C]]

[[Category: Sanford, D G]]

[[Category: Transmembrane]]