1esl

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(New page: 200px<br /> <applet load="1esl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esl, resolution 2.0&Aring;" /> '''INSIGHT INTO E-SELEC...)
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'''INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS'''<br />
'''INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS'''<br />
==Overview==
==Overview==
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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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1ESL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESL OCA].
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1ESL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESL OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Crowther, R.L.]]
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[[Category: Crowther, R L.]]
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[[Category: Graves, B.J.]]
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[[Category: Graves, B J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CL]]
[[Category: CL]]
[[Category: cell adhesion protein]]
[[Category: cell adhesion protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:46:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:06 2008''

Revision as of 10:31, 21 February 2008


1esl, resolution 2.0Å

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

Contents

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.

Disease

Known diseases associated with this structure: Atherosclerosis, susceptibility to OMIM:[131210], Blood pressure regulation QTL OMIM:[131210], IgA nephropathy, susceptiblity to OMIM:[131210]

About this Structure

1ESL is a Single protein structure of sequence from Homo sapiens with and as ligands. 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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