1h6t

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{{Seed}}
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{{STRUCTURE_1h6t| PDB=1h6t | SCENE= }}
{{STRUCTURE_1h6t| PDB=1h6t | SCENE= }}
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'''INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.'''
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===INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.===
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==Overview==
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Listeria monocytogenes is an opportunistic, food-borne human and animal pathogen. Host cell invasion requires the action of the internalins A (InlA) and B (InlB), which are members of a family of listerial cell-surface proteins. Common to these proteins are three distinctive N-terminal domains that have been shown to direct host cell-specific invasion for InlA and InlB. Here, we present the high-resolution crystal structures of these domains present in InlB and InlH, and show that they constitute a single "internalin domain". In this internalin domain, a central LRR region is flanked contiguously by a truncated EF-hand-like cap and an immunoglobulin (Ig)-like fold. The extended beta-sheet, resulting from the distinctive fusion of the LRR and the Ig-like folds, constitutes an adaptable concave interaction surface, which we propose is responsible for the specific recognition of the host cellular binding partners during infection.
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(as it appears on PubMed at http://www.pubmed.gov), where 11575932 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11575932}}
==About this Structure==
==About this Structure==
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[[Category: Ig-like domain]]
[[Category: Ig-like domain]]
[[Category: Leucine rich repeat]]
[[Category: Leucine rich repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:30:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:43:12 2008''

Revision as of 03:43, 1 July 2008

Image:1h6t.png

Template:STRUCTURE 1h6t

INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.

Template:ABSTRACT PUBMED 11575932

About this Structure

1H6T is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain., Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW, J Mol Biol. 2001 Sep 28;312(4):783-94. PMID:11575932

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