1g1q

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(New page: 200px<br /> <applet load="1g1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1q, resolution 2.4&Aring;" /> '''Crystal structure of...)
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<applet load="1g1q" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1g1q, resolution 2.4&Aring;" />
caption="1g1q, resolution 2.4&Aring;" />
'''Crystal structure of P-selectin lectin/EGF domains'''<br />
'''Crystal structure of P-selectin lectin/EGF domains'''<br />
==Overview==
==Overview==
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P-, E- and L-selectin constitute a family of cell adhesion receptors that, mediate the initial tethering and rolling of leukocytes on inflamed, endothelium as a prelude to their firm attachment and extravasation into, tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and, E-selectin constructs containing the lectin and EGF (LE) domains, co-complexed with SLe(X). We also present the crystal structure of, P-selectin LE co-complexed with the N-terminal domain of human PSGL-1, modified by both tyrosine sulfation and SLe(X). These structures reveal, differences in how E- and P-selectin bind SLe(X) and the molecular basis, of the high-affinity interaction between P-selectin and PSGL-1.
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P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X). We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X). These structures reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1G1Q 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 MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1Q OCA].
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1G1Q 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=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Q OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Camphausen, R.T.]]
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[[Category: Camphausen, R T.]]
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[[Category: Somers, W.S.]]
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[[Category: Somers, W S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MRD]]
[[Category: MRD]]
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[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:59:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:05 2008''

Revision as of 10:45, 21 February 2008

Image:1g1q.gif

1g1q, resolution 2.4Å

Drag the structure with the mouse to rotate

Crystal structure of P-selectin lectin/EGF domains

Contents

Overview

P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X). We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X). These structures reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.

Disease

Known diseases associated with this structure: Atopy, susceptibility to OMIM:[173610], Platelet alpha/delta storage pool deficiency OMIM:[173610]

About this Structure

1G1Q is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1., Somers WS, Tang J, Shaw GD, Camphausen RT, Cell. 2000 Oct 27;103(3):467-79. PMID:11081633

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