1yuk: Difference between revisions

Revision as of 13:45, 28 July 2008

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File:1yuk.png

Template:STRUCTURE 1yuk

The crystal structure of the PSI/Hybrid domain/ I-EGF1 segment from the human integrin beta2 at 1.8 resolutionThe crystal structure of the PSI/Hybrid domain/ I-EGF1 segment from the human integrin beta2 at 1.8 resolution

Template:ABSTRACT PUBMED 15965234

About this StructureAbout this Structure

1YUK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the plexin-semaphorin-integrin domain/hybrid domain/I-EGF1 segment from the human integrin beta2 subunit at 1.8-A resolution., Shi M, Sundramurthy K, Liu B, Tan SM, Law SK, Lescar J, J Biol Chem. 2005 Aug 26;280(34):30586-93. Epub 2005 Jun 17. PMID:15965234

Page seeded by OCA on Mon Jul 28 13:45:39 2008

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

OCA

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-[[Image:1yuk.gif|left|200px]]
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 {{STRUCTURE_1yuk|  PDB=1yuk  |  SCENE=  }}
-'''The crystal structure of the PSI/Hybrid domain/ I-EGF1 segment from the human integrin beta2 at 1.8 resolution'''
+===The crystal structure of the PSI/Hybrid domain/ I-EGF1 segment from the human integrin beta2 at 1.8 resolution===
-==Overview==
+<!--
-Integrins are modular (alphabeta) heterodimeric proteins that mediate cell adhesion and convey signals across the plasma membrane. Interdomain motions play a key role in signal transduction by propagating structural changes through the molecule, thus controlling the activation state and adhesive properties of the integrin. We expressed a soluble fragment of the human integrin beta2 subunit comprising the plexin-semaphorin-integrin domain (PSI)/hybrid domain/I-EGF1 fragment and present its crystal structure at 1.8-A resolution. The structure reveals an elongated molecule with a rigid architecture stabilized by nine disulfide bridges. The PSI domain is located centrally and participates in the formation of extended interfaces with the hybrid domain and I-EGF1 domains, respectively. The hybrid domain/PSI interface involves the burial of an Arg residue, and contacts between PSI and I-EGF1 are mainly mediated by well conserved Arg and Trp residues. Conservation of key interacting residues across the various integrin beta subunits sequences suggests that our structure represents a good model for the entire integrin family. Superposition with the integrin beta3 receptor in its bent conformation suggests that an articulation point is present at the linkage between its I-EGF1 and I-EGF2 modules and underlines the importance of this region for the control of integrin-mediated cell adhesion.
+The line below this paragraph, {{ABSTRACT_PUBMED_15965234}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15965234 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15965234}}
 ==About this Structure==
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 [[Category: Integrin beta2]]
 [[Category: Psi domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:48:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:45:39 2008''