1z78: Difference between revisions

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New page: left|200px<br /> <applet load="1z78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z78, resolution 1.8Å" /> '''Crystal Structure of...
 
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[[Image:1z78.gif|left|200px]]<br />
[[Image:1z78.gif|left|200px]]<br /><applet load="1z78" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1z78" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1z78, resolution 1.8&Aring;" />
caption="1z78, resolution 1.8&Aring;" />
'''Crystal Structure of the Thrombospondin-1 N-terminal domain'''<br />
'''Crystal Structure of the Thrombospondin-1 N-terminal domain'''<br />


==Overview==
==Overview==
The N-terminal domain of thrombospondin-1 (TSPN-1) mediates the protein's, interaction with (1) glycosaminoglycans, calreticulin, and integrins, during cellular adhesion, (2) low-density lipoprotein receptor-related, protein during uptake and clearance, and (3) fibrinogen during platelet, aggregation. The crystal structure of TSPN-1 to 1.8 A resolution is a beta, sandwich with 13 antiparallel beta strands and 1 irregular strand-like, segment. Unique structural features of the N- and C-terminal regions, and, the disulfide bond location, distinguish TSPN-1 from the laminin G domain, and other concanavalin A-like lectins/glucanases superfamily members. The, crystal structure of the complex of TSPN-1 with heparin indicates that, residues R29, R42, and R77 in an extensive positively charged patch at the, bottom of the domain specifically associate with the sulfate groups of, heparin. The TSPN-1 structure and identified adjacent linker region, provide a structural framework for the analysis of the TSPN domain of, various molecules, including TSPs, NELLs, many collagens, TSPEAR, and, kielin.
The N-terminal domain of thrombospondin-1 (TSPN-1) mediates the protein's interaction with (1) glycosaminoglycans, calreticulin, and integrins during cellular adhesion, (2) low-density lipoprotein receptor-related protein during uptake and clearance, and (3) fibrinogen during platelet aggregation. The crystal structure of TSPN-1 to 1.8 A resolution is a beta sandwich with 13 antiparallel beta strands and 1 irregular strand-like segment. Unique structural features of the N- and C-terminal regions, and the disulfide bond location, distinguish TSPN-1 from the laminin G domain and other concanavalin A-like lectins/glucanases superfamily members. The crystal structure of the complex of TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive positively charged patch at the bottom of the domain specifically associate with the sulfate groups of heparin. The TSPN-1 structure and identified adjacent linker region provide a structural framework for the analysis of the TSPN domain of various molecules, including TSPs, NELLs, many collagens, TSPEAR, and kielin.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1Z78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z78 OCA].  
1Z78 is a [http://en.wikipedia.org/wiki/Single_protein 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=1Z78 OCA].  


==Reference==
==Reference==
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[[Category: tsp-1]]
[[Category: tsp-1]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:44 2008''

Revision as of 17:12, 21 February 2008

File:1z78.gif


1z78, resolution 1.8Å

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Crystal Structure of the Thrombospondin-1 N-terminal domain

OverviewOverview

The N-terminal domain of thrombospondin-1 (TSPN-1) mediates the protein's interaction with (1) glycosaminoglycans, calreticulin, and integrins during cellular adhesion, (2) low-density lipoprotein receptor-related protein during uptake and clearance, and (3) fibrinogen during platelet aggregation. The crystal structure of TSPN-1 to 1.8 A resolution is a beta sandwich with 13 antiparallel beta strands and 1 irregular strand-like segment. Unique structural features of the N- and C-terminal regions, and the disulfide bond location, distinguish TSPN-1 from the laminin G domain and other concanavalin A-like lectins/glucanases superfamily members. The crystal structure of the complex of TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive positively charged patch at the bottom of the domain specifically associate with the sulfate groups of heparin. The TSPN-1 structure and identified adjacent linker region provide a structural framework for the analysis of the TSPN domain of various molecules, including TSPs, NELLs, many collagens, TSPEAR, and kielin.

DiseaseDisease

Known disease associated with this structure: Sudden infant death with dysgenesis of the testes syndrome OMIM:[604714]

About this StructureAbout this Structure

1Z78 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin., Tan K, Duquette M, Liu JH, Zhang R, Joachimiak A, Wang JH, Lawler J, Structure. 2006 Jan;14(1):33-42. PMID:16407063

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