1esl

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|PDB= 1esl |SIZE=350|CAPTION= <scene name='initialview01'>1esl</scene>, resolution 2.0&Aring;
|PDB= 1esl |SIZE=350|CAPTION= <scene name='initialview01'>1esl</scene>, resolution 2.0&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1esl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esl OCA], [http://www.ebi.ac.uk/pdbsum/1esl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1esl RCSB]</span>
}}
}}
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==Overview==
==Overview==
The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.
The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.
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==Disease==
 
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Known diseases associated with this structure: Atherosclerosis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131210 131210]], Blood pressure regulation QTL OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131210 131210]], IgA nephropathy, susceptiblity to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131210 131210]]
 
==About this Structure==
==About this Structure==
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[[Category: Crowther, R L.]]
[[Category: Crowther, R L.]]
[[Category: Graves, B J.]]
[[Category: Graves, B J.]]
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[[Category: CA]]
 
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[[Category: CL]]
 
[[Category: cell adhesion protein]]
[[Category: cell adhesion protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:47 2008''

Revision as of 17:08, 30 March 2008


PDB ID 1esl

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS


Overview

The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.

About this Structure

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

Reference

Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains., Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang KS, Presky DH, Familletti PC, Wolitzky BA, Burns DK, Nature. 1994 Feb 10;367(6463):532-8. PMID:7509040

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