1z78: Difference between revisions

Revision as of 08:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z78.png

Template:STRUCTURE 1z78

Crystal Structure of the Thrombospondin-1 N-terminal domainCrystal Structure of the Thrombospondin-1 N-terminal domain

Template:ABSTRACT PUBMED 16407063

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

Page seeded by OCA on Mon Jul 28 08:40:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1z78.gif|left|200px]]
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 {{STRUCTURE_1z78|  PDB=1z78  |  SCENE=  }}
-'''Crystal Structure of the Thrombospondin-1 N-terminal domain'''
+===Crystal Structure of the Thrombospondin-1 N-terminal domain===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_16407063}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16407063 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16407063}}
 ==About this Structure==
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 [[Category: Ntsp-1]]
 [[Category: Tsp-1]]
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