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| - | [[Image:1lmt.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1lmt| PDB=1lmt | SCENE= }} | | {{STRUCTURE_1lmt| PDB=1lmt | SCENE= }} |
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| - | '''STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME'''
| + | ===STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME=== |
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| - | ==Overview==
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| - | To examine the effect of a conformational constraint introduced into the Arg-Gly-Asp (RGD) sequence on cell adhesion activity, we constructed a mutant protein by inserting an RGD-containing sequence flanked by two Cys residues between Val74 and Asn75 of human lysozyme. The CRGDSC-inserted lysozyme was expressed in yeast, purified, and designated as Cys-RGD4. Using baby hamster kidney cells, Cys-RGD4 was shown to possess even higher cell adhesion activity than that of the RGDS-inserted lysozyme, RGD4. The Cys-RGD4 protein was co-crystallized with a lysozyme inhibitor, tri-N-acetylchitotriose, and the three-dimensional structure was determined at 1.6-A resolution by x-ray crystallography. In contrast to RGD4, the inserted RGD-containing region of Cys-RGD4 was well defined. The structural analysis revealed that the two inserted Cys residues form a new disulfide bond in Cys-RGD4, as expected, and that the RGD region assumes a type II' beta-turn conformation of Gly-Asp with a hydrogen bond between the C = O of Arg and the H-N of Ser. In addition, it was confirmed that two more hydrogen bonds are present in the RGD region of the Cys-RGD4 lysozyme. These results suggest that the conformation of the RGD-containing region is rigid and stable in the Cys-RGD4 molecule and that the type II' beta-turn structure of RGD is essential for binding to integrins with high affinity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7890692}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7890692 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7890692}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Matsushima, M.]] | | [[Category: Matsushima, M.]] |
| | [[Category: Song, H.]] | | [[Category: Song, H.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:04:31 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:27:14 2008'' |
Revision as of 18:27, 2 July 2008
Template:STRUCTURE 1lmt
STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME
Template:ABSTRACT PUBMED 7890692
About this Structure
1LMT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme., Yamada T, Song H, Inaka K, Shimada Y, Kikuchi M, Matsushima M, J Biol Chem. 1995 Mar 17;270(11):5687-90. PMID:7890692
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