1q7d

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(New page: 200px<br /> <applet load="1q7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q7d, resolution 1.8&Aring;" /> '''Structure of the int...)
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[[Image:1q7d.gif|left|200px]]<br /><applet load="1q7d" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1q7d" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1q7d, resolution 1.8&Aring;" />
caption="1q7d, resolution 1.8&Aring;" />
'''Structure of the integrin alpha2beta1 binding collagen peptide'''<br />
'''Structure of the integrin alpha2beta1 binding collagen peptide'''<br />
==Overview==
==Overview==
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We have determined the 1.8A crystal structure of a triple helical, integrin-binding collagen peptide (IBP) with sequence, (Gly-Pro-Hyp)(2)-Gly-Phe-Hyp-Gly-Glu-Arg-(Gly-Pro-Hyp)(3). The central, GFOGER hexapeptide is recognised specifically by the integrins, alpha2beta1, alpha1beta1, alpha10beta1 and alpha11beta1. These, integrin/collagen interactions are implicated in a number of key, physiological processes including cell adhesion, cell growth and, differentiation, and pathological states such as thrombosis and tumour, metastasis. Comparison of the IBP structure with the previously determined, structure of an identical collagen peptide in complex with the integrin, alpha2-I domain (IBP(c)) allows the first detailed examination of collagen, in a bound and an unbound state. The IBP structure shows a direct and a, water-mediated electrostatic interaction between Glu and Arg side-chains, from adjacent strands, but no intra-strand interactions. The interactions, between IBP Glu and Arg side-chains are disrupted upon integrin binding. A, comparison of IBP and IBP(c) main-chain conformation reveals the flexible, nature of the triple helix backbone in the imino-poor GFOGER region. This, flexibility could be important to the integrin-collagen interaction and, provides a possible explanation for the unique orientation of the three, GFOGER strands observed in the integrin-IBP(c) complex crystal structure.
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We have determined the 1.8A crystal structure of a triple helical integrin-binding collagen peptide (IBP) with sequence (Gly-Pro-Hyp)(2)-Gly-Phe-Hyp-Gly-Glu-Arg-(Gly-Pro-Hyp)(3). The central GFOGER hexapeptide is recognised specifically by the integrins alpha2beta1, alpha1beta1, alpha10beta1 and alpha11beta1. These integrin/collagen interactions are implicated in a number of key physiological processes including cell adhesion, cell growth and differentiation, and pathological states such as thrombosis and tumour metastasis. Comparison of the IBP structure with the previously determined structure of an identical collagen peptide in complex with the integrin alpha2-I domain (IBP(c)) allows the first detailed examination of collagen in a bound and an unbound state. The IBP structure shows a direct and a water-mediated electrostatic interaction between Glu and Arg side-chains from adjacent strands, but no intra-strand interactions. The interactions between IBP Glu and Arg side-chains are disrupted upon integrin binding. A comparison of IBP and IBP(c) main-chain conformation reveals the flexible nature of the triple helix backbone in the imino-poor GFOGER region. This flexibility could be important to the integrin-collagen interaction and provides a possible explanation for the unique orientation of the three GFOGER strands observed in the integrin-IBP(c) complex crystal structure.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1Q7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q7D OCA].
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1Q7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7D OCA].
==Reference==
==Reference==
Structure of the integrin alpha2beta1-binding collagen peptide., Emsley J, Knight CG, Farndale RW, Barnes MJ, J Mol Biol. 2004 Jan 23;335(4):1019-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14698296 14698296]
Structure of the integrin alpha2beta1-binding collagen peptide., Emsley J, Knight CG, Farndale RW, Barnes MJ, J Mol Biol. 2004 Jan 23;335(4):1019-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14698296 14698296]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barnes, M.J.]]
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[[Category: Barnes, M J.]]
[[Category: Emsley, J.]]
[[Category: Emsley, J.]]
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[[Category: Farndale, R.W.]]
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[[Category: Farndale, R W.]]
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[[Category: Knight, C.G.]]
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[[Category: Knight, C G.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: NH2]]
[[Category: NH2]]
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[[Category: triplehelix]]
[[Category: triplehelix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:51:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:37 2008''

Revision as of 12:36, 21 February 2008

Image:1q7d.gif

1q7d, resolution 1.8Å

Drag the structure with the mouse to rotate

Structure of the integrin alpha2beta1 binding collagen peptide

Contents

Overview

We have determined the 1.8A crystal structure of a triple helical integrin-binding collagen peptide (IBP) with sequence (Gly-Pro-Hyp)(2)-Gly-Phe-Hyp-Gly-Glu-Arg-(Gly-Pro-Hyp)(3). The central GFOGER hexapeptide is recognised specifically by the integrins alpha2beta1, alpha1beta1, alpha10beta1 and alpha11beta1. These integrin/collagen interactions are implicated in a number of key physiological processes including cell adhesion, cell growth and differentiation, and pathological states such as thrombosis and tumour metastasis. Comparison of the IBP structure with the previously determined structure of an identical collagen peptide in complex with the integrin alpha2-I domain (IBP(c)) allows the first detailed examination of collagen in a bound and an unbound state. The IBP structure shows a direct and a water-mediated electrostatic interaction between Glu and Arg side-chains from adjacent strands, but no intra-strand interactions. The interactions between IBP Glu and Arg side-chains are disrupted upon integrin binding. A comparison of IBP and IBP(c) main-chain conformation reveals the flexible nature of the triple helix backbone in the imino-poor GFOGER region. This flexibility could be important to the integrin-collagen interaction and provides a possible explanation for the unique orientation of the three GFOGER strands observed in the integrin-IBP(c) complex crystal structure.

Disease

Known diseases associated with this structure: Caffey disease OMIM:[120150], Dissection of cervical arteries OMIM:[120150], Ehlers-Danlos syndrome, type I OMIM:[120150], Ehlers-Danlos syndrome, type VII OMIM:[120150], OI type II OMIM:[120150], OI type III OMIM:[120150], OI type IV OMIM:[120150], OI/EDS combined syndrome OMIM:[120150], Osteogenesis imperfecta, type I OMIM:[120150], Osteoporosis OMIM:[120150]

About this Structure

1Q7D is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the integrin alpha2beta1-binding collagen peptide., Emsley J, Knight CG, Farndale RW, Barnes MJ, J Mol Biol. 2004 Jan 23;335(4):1019-28. PMID:14698296

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